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Volumn 1818, Issue 4, 2012, Pages 1067-1084

The Bam machine: A molecular cooper

Author keywords

barrel; Bam complex; LPS; Outer membrane biogenesis

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; CHAPERONE; COPPER; LIPOPROTEIN; MULTIPROTEIN COMPLEX; OUTER MEMBRANE PROTEIN; PEPTIDOGLYCAN; PHOSPHOLIPID; PROTEIN BAM; PROTEIN BAMA; PROTEIN BAMB; PROTEIN BAMC; PROTEIN BAMD; PROTEIN BAME; UNCLASSIFIED DRUG;

EID: 84857644824     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.08.020     Document Type: Review
Times cited : (138)

References (203)
  • 2
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • M.W. Gray, G. Burger, and B.F. Lang Mitochondrial evolution Science 283 1999 1476 1481
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 3
    • 0017174518 scopus 로고
    • Distribution of lipids in cytoplasmic and outer membranes of Escherichia coli K12
    • E.J. Lugtenberg, and R. Peters Distribution of lipids in cytoplasmic and outer membranes of Escherichia coli K12 Biochim. Biophys. Acta 441 1976 38 47
    • (1976) Biochim. Biophys. Acta , vol.441 , pp. 38-47
    • Lugtenberg, E.J.1    Peters, R.2
  • 5
    • 0017188213 scopus 로고
    • Outer membrane of Salmonella typhimurium: Accessibility of phospholipid head groups to phospholipase c and cyanogen bromide activated dextran in the external medium
    • Y. Kamio, and H. Nikaido Outer membrane of Salmonella typhimurium: accessibility of phospholipid head groups to phospholipase c and cyanogen bromide activated dextran in the external medium Biochemistry 15 1976 2561 2570
    • (1976) Biochemistry , vol.15 , pp. 2561-2570
    • Kamio, Y.1    Nikaido, H.2
  • 6
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • H. Nikaido Molecular basis of bacterial outer membrane permeability revisited Microbiol. Mol. Biol. Rev. 67 2003 593 656
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 8
    • 33646594697 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in three cell environments in Escherichia coli
    • C.W. Mullineaux, A. Nenninger, N. Ray, and C. Robinson Diffusion of green fluorescent protein in three cell environments in Escherichia coli J. Bacteriol. 188 2006 3442 3448
    • (2006) J. Bacteriol. , vol.188 , pp. 3442-3448
    • Mullineaux, C.W.1    Nenninger, A.2    Ray, N.3    Robinson, C.4
  • 9
    • 4544222062 scopus 로고    scopus 로고
    • Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm
    • H. Miyadai, K. Tanaka-Masuda, S.-i. Matsuyama, and H. Tokuda Effects of lipoprotein overproduction on the induction of DegP (HtrA) involved in quality control in the Escherichia coli periplasm J. Biol. Chem. 279 2004 39807 39813
    • (2004) J. Biol. Chem. , vol.279 , pp. 39807-39813
    • Miyadai, H.1    Tanaka-Masuda, K.2    Matsuyama, S.-I.3    Tokuda, H.4
  • 10
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • T. Wu, J. Malinverni, N. Ruiz, S. Kim, T.J. Silhavy, and D. Kahne Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli Cell 121 2005 235 245
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6
  • 11
    • 33745202589 scopus 로고    scopus 로고
    • YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
    • J.C. Malinverni, J. Werner, S. Kim, J.G. Sklar, D. Kahne, R. Misra, and T.J. Silhavy YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli Mol. Microbiol. 61 2006 151 164
    • (2006) Mol. Microbiol. , vol.61 , pp. 151-164
    • Malinverni, J.C.1    Werner, J.2    Kim, S.3    Sklar, J.G.4    Kahne, D.5    Misra, R.6    Silhavy, T.J.7
  • 12
    • 33746852673 scopus 로고    scopus 로고
    • Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli
    • T. Wu, A.C. McCandlish, L.S. Gronenberg, S.-S. Chng, T.J. Silhavy, and D. Kahne Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 103 2006 11754 11759
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 11754-11759
    • Wu, T.1    McCandlish, A.C.2    Gronenberg, L.S.3    Chng, S.-S.4    Silhavy, T.J.5    Kahne, D.6
  • 15
    • 67749117916 scopus 로고    scopus 로고
    • LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli
    • T. Uehara, T. Dinh, and T.G. Bernhardt LytM-domain factors are required for daughter cell separation and rapid ampicillin-induced lysis in Escherichia coli J. Bacteriol. 191 2009 5094 5107
    • (2009) J. Bacteriol. , vol.191 , pp. 5094-5107
    • Uehara, T.1    Dinh, T.2    Bernhardt, T.G.3
  • 16
    • 79955027962 scopus 로고    scopus 로고
    • Sorting of an integral outer membrane protein via the lipoprotein-specific Lol pathway and a dedicated lipoprotein pilotin
    • S. Collin, I. Guilvout, N.N. Nickerson, and A.P. Pugsley Sorting of an integral outer membrane protein via the lipoprotein-specific Lol pathway and a dedicated lipoprotein pilotin Mol. Microbiol. 80 2011 655 665
    • (2011) Mol. Microbiol. , vol.80 , pp. 655-665
    • Collin, S.1    Guilvout, I.2    Nickerson, N.N.3    Pugsley, A.P.4
  • 17
    • 40449091818 scopus 로고    scopus 로고
    • The Rcs phosphorelay is a cell envelope stress response activated by peptidoglycan stress and contributes to intrinsic antibiotic resistance
    • M.E. Laubacher, and S.E. Ades The Rcs phosphorelay is a cell envelope stress response activated by peptidoglycan stress and contributes to intrinsic antibiotic resistance J. Bacteriol. 190 2008 2065 2074
    • (2008) J. Bacteriol. , vol.190 , pp. 2065-2074
    • Laubacher, M.E.1    Ades, S.E.2
  • 18
    • 77950438894 scopus 로고    scopus 로고
    • Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane
    • S.-S. Chng, N. Ruiz, G. Chimalakonda, T.J. Silhavy, and D. Kahne Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane Proc. Natl. Acad. Sci. U.S.A. 107 2010 5363 5368
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5363-5368
    • Chng, S.-S.1    Ruiz, N.2    Chimalakonda, G.3    Silhavy, T.J.4    Kahne, D.5
  • 19
    • 68749109764 scopus 로고    scopus 로고
    • Dissection of LolB function-lipoprotein binding, membrane targeting and incorporation of lipoproteins into lipid bilayers
    • J. Tsukahara, K. Mukaiyama, S. Okuda, S. Narita, and H. Tokuda Dissection of LolB function-lipoprotein binding, membrane targeting and incorporation of lipoproteins into lipid bilayers FEBS J. 276 2009 4496 4504
    • (2009) FEBS J. , vol.276 , pp. 4496-4504
    • Tsukahara, J.1    Mukaiyama, K.2    Okuda, S.3    Narita, S.4    Tokuda, H.5
  • 20
    • 0031002073 scopus 로고    scopus 로고
    • Lethality of the covalent linkage between mislocalized major outer membrane lipoprotein and the peptidoglycan of Escherichia coli
    • T. Yakushi, T. Tajima, S. Matsuyama, and H. Tokuda Lethality of the covalent linkage between mislocalized major outer membrane lipoprotein and the peptidoglycan of Escherichia coli J. Bacteriol. 179 1997 2857 2862
    • (1997) J. Bacteriol. , vol.179 , pp. 2857-2862
    • Yakushi, T.1    Tajima, T.2    Matsuyama, S.3    Tokuda, H.4
  • 21
    • 0041428149 scopus 로고    scopus 로고
    • The versatile beta-barrel membrane protein
    • W.C. Wimley The versatile beta-barrel membrane protein Curr. Opin. Struct. Biol. 13 2003 404 411
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 22
    • 7044247850 scopus 로고    scopus 로고
    • Folding and assembly of beta-barrel membrane proteins
    • L.K. Tamm, H. Hong, and B. Liang Folding and assembly of beta-barrel membrane proteins Biochim. Biophys. Acta 1666 2004 250 263
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 250-263
    • Tamm, L.K.1    Hong, H.2    Liang, B.3
  • 23
    • 78049291824 scopus 로고    scopus 로고
    • Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily
    • A.S. Delattre, B. Clantin, N. Saint, C. Locht, V. Villeret, and F. Jacob-Dubuisson Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily FEBS J 277 2010 4755 4765
    • (2010) FEBS J , vol.277 , pp. 4755-4765
    • Delattre, A.S.1    Clantin, B.2    Saint, N.3    Locht, C.4    Villeret, V.5    Jacob-Dubuisson, F.6
  • 24
    • 0000983237 scopus 로고    scopus 로고
    • In vitro folding, purification and characterization of Escherichia coli outer membrane protease ompT
    • R.A. Kramer, D. Zandwijken, M.R. Egmond, and N. Dekker In vitro folding, purification and characterization of Escherichia coli outer membrane protease ompT Eur. J. Biochem. 267 2000 885 893
    • (2000) Eur. J. Biochem. , vol.267 , pp. 885-893
    • Kramer, R.A.1    Zandwijken, D.2    Egmond, M.R.3    Dekker, N.4
  • 27
    • 33746356503 scopus 로고    scopus 로고
    • Biosynthesis and assembly of capsular polysaccharides in Escherichia coli
    • C. Whitfield Biosynthesis and assembly of capsular polysaccharides in Escherichia coli Annu. Rev. Biochem. 75 2006 39 68
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 39-68
    • Whitfield, C.1
  • 28
    • 0035094251 scopus 로고    scopus 로고
    • Molecular sieve mechanism of selective release of cytoplasmic proteins by osmotically shocked Escherichia coli
    • N. Vázquez-Laslop, H. Lee, R. Hu, and A.A. Neyfakh Molecular sieve mechanism of selective release of cytoplasmic proteins by osmotically shocked Escherichia coli J. Bacteriol. 183 2001 2399 2404
    • (2001) J. Bacteriol. , vol.183 , pp. 2399-2404
    • Vázquez-Laslop, N.1    Lee, H.2    Hu, R.3    Neyfakh, A.A.4
  • 30
    • 0027285690 scopus 로고
    • Signal sequence processing is required for the assembly of LamB trimers in the outer membrane of Escherichia coli
    • J.H. Carlson, and T.J. Silhavy Signal sequence processing is required for the assembly of LamB trimers in the outer membrane of Escherichia coli J. Bacteriol. 175 1993 3327 3334
    • (1993) J. Bacteriol. , vol.175 , pp. 3327-3334
    • Carlson, J.H.1    Silhavy, T.J.2
  • 31
    • 33751086145 scopus 로고    scopus 로고
    • Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin
    • I. Guilvout, M. Chami, A. Engel, A.P. Pugsley, and N. Bayan Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin EMBO J. 25 2006 5241 5249
    • (2006) EMBO J. , vol.25 , pp. 5241-5249
    • Guilvout, I.1    Chami, M.2    Engel, A.3    Pugsley, A.P.4    Bayan, N.5
  • 32
    • 79959468179 scopus 로고    scopus 로고
    • β-Barrel membrane protein assembly by the bam complex
    • C.L. Hagan, T.J. Silhavy, and D.E. Kahne β-Barrel membrane protein assembly by the bam complex Annu. Rev. Biochem. 80 2010 189 210
    • (2010) Annu. Rev. Biochem. , vol.80 , pp. 189-210
    • Hagan, C.L.1    Silhavy, T.J.2    Kahne, D.E.3
  • 33
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the Gram-negative bacterial outer membrane
    • M.P. Bos, V. Robert, and J. Tommassen Biogenesis of the Gram-negative bacterial outer membrane Annu. Rev. Microbiol. 61 2007 191 214
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 34
    • 67649289353 scopus 로고    scopus 로고
    • The lipopolysaccharide transport system of Gram-negative bacteria
    • P. Sperandeo, G. Dehò, and A. Polissi The lipopolysaccharide transport system of Gram-negative bacteria Biochim. Biophys. Acta 1791 2009 594 602
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 594-602
    • Sperandeo, P.1    Dehò, G.2    Polissi, A.3
  • 35
    • 67649367532 scopus 로고    scopus 로고
    • Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides
    • S.-i. Narita, and H. Tokuda Biochemical characterization of an ABC transporter LptBFGC complex required for the outer membrane sorting of lipopolysaccharides FEBS Lett. 583 2009 2160 2164
    • (2009) FEBS Lett. , vol.583 , pp. 2160-2164
    • Narita, S.-I.1    Tokuda, H.2
  • 36
    • 44449176988 scopus 로고    scopus 로고
    • Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli
    • N. Ruiz, L.S. Gronenberg, D. Kahne, and T.J. Silhavy Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 105 2008 5537 5542
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 5537-5542
    • Ruiz, N.1    Gronenberg, L.S.2    Kahne, D.3    Silhavy, T.J.4
  • 37
    • 79951599665 scopus 로고    scopus 로고
    • New insights into the Lpt machinery for lipopolysaccharide transport to the cell surface: LptA-LptC interaction and LptA stability as sensors of a properly assembled transenvelope complex
    • P. Sperandeo, R. Villa, A.M. Martorana, M. Samalikova, R. Grandori, G. Dehò, and A. Polissi New insights into the Lpt machinery for lipopolysaccharide transport to the cell surface: LptA-LptC interaction and LptA stability as sensors of a properly assembled transenvelope complex J. Bacteriol. 193 2011 1042 1053
    • (2011) J. Bacteriol. , vol.193 , pp. 1042-1053
    • Sperandeo, P.1    Villa, R.2    Martorana, A.M.3    Samalikova, M.4    Grandori, R.5    Dehò, G.6    Polissi, A.7
  • 38
    • 77958502198 scopus 로고    scopus 로고
    • Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli
    • A.X. Tran, C. Dong, and C. Whitfield Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli J. Biol. Chem. 285 2010 33529 33539
    • (2010) J. Biol. Chem. , vol.285 , pp. 33529-33539
    • Tran, A.X.1    Dong, C.2    Whitfield, C.3
  • 39
    • 51749125875 scopus 로고    scopus 로고
    • Novel structure of the conserved Gram-negative lipopolysaccharide transport protein A and mutagenesis analysis
    • M.D.L. Suits, P. Sperandeo, G. Dehò, A. Polissi, and Z. Jia Novel structure of the conserved Gram-negative lipopolysaccharide transport protein A and mutagenesis analysis J. Mol. Biol. 380 2008 476 488
    • (2008) J. Mol. Biol. , vol.380 , pp. 476-488
    • Suits, M.D.L.1    Sperandeo, P.2    Dehò, G.3    Polissi, A.4    Jia, Z.5
  • 40
    • 77953084208 scopus 로고    scopus 로고
    • Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex
    • S.-S. Chng, L.S. Gronenberg, and D. Kahne Proteins required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex Biochemistry 49 2010 4565 4567
    • (2010) Biochemistry , vol.49 , pp. 4565-4567
    • Chng, S.-S.1    Gronenberg, L.S.2    Kahne, D.3
  • 41
    • 79952289193 scopus 로고    scopus 로고
    • The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel
    • E. Freinkman, S.-S. Chng, and D. Kahne The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel Proc. Natl. Acad. Sci. U.S.A. 108 2011 2486 2491
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2486-2491
    • Freinkman, E.1    Chng, S.-S.2    Kahne, D.3
  • 42
    • 77954373738 scopus 로고    scopus 로고
    • Going forward laterally: Transmembrane passage of hydrophobic molecules through protein channel walls
    • B. van den Berg Going forward laterally: transmembrane passage of hydrophobic molecules through protein channel walls Chembiochem 11 2010 1339 1343
    • (2010) Chembiochem , vol.11 , pp. 1339-1343
    • Van Den Berg, B.1
  • 43
    • 0035853703 scopus 로고    scopus 로고
    • An Escherichia coli mutant defective in lipid export
    • W.T. Doerrler An Escherichia coli mutant defective in lipid export J. Biol. Chem. 276 2001 11461 11464
    • (2001) J. Biol. Chem. , vol.276 , pp. 11461-11464
    • Doerrler, W.T.1
  • 45
    • 0041589300 scopus 로고    scopus 로고
    • Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane
    • M.A. Kol, A. van Dalen, A.I.P.M. de Kroon, and B. de Kruijff Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane J. Biol. Chem. 278 2003 24586 24593
    • (2003) J. Biol. Chem. , vol.278 , pp. 24586-24593
    • Kol, M.A.1    Van Dalen, A.2    De Kroon, A.I.P.M.3    De Kruijff, B.4
  • 47
    • 0014346151 scopus 로고
    • Areas of adhesion between wall and membrane of Escherichia coli
    • M.E. Bayer Areas of adhesion between wall and membrane of Escherichia coli J. Gen. Microbiol. 53 1968 395 404
    • (1968) J. Gen. Microbiol. , vol.53 , pp. 395-404
    • Bayer, M.E.1
  • 48
    • 0026318173 scopus 로고
    • Zones of membrane adhesion in the cryofixed envelope of Escherichia coli
    • M.E. Bayer Zones of membrane adhesion in the cryofixed envelope of Escherichia coli J. Struct. Biol. 107 1991 268 280
    • (1991) J. Struct. Biol. , vol.107 , pp. 268-280
    • Bayer, M.E.1
  • 49
    • 0025314999 scopus 로고
    • The 'Bayer bridges' confronted with results from improved electron microscopy methods
    • E. Kellenberger The 'Bayer bridges' confronted with results from improved electron microscopy methods Mol. Microbiol. 4 1990 697 705
    • (1990) Mol. Microbiol. , vol.4 , pp. 697-705
    • Kellenberger, E.1
  • 50
    • 0018893142 scopus 로고
    • Translocation of phospholipids from the inner to the outer membrane of Escherichia coli
    • A.M. Donohue-Rolfe, and M. Schaechter Translocation of phospholipids from the inner to the outer membrane of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 77 1980 1867 1871
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 1867-1871
    • Donohue-Rolfe, A.M.1    Schaechter, M.2
  • 51
    • 78649967779 scopus 로고    scopus 로고
    • Lipid trafficking sans vesicles: Where, why, how?
    • W.A. Prinz Lipid trafficking sans vesicles: where, why, how? Cell 143 2010 870 874
    • (2010) Cell , vol.143 , pp. 870-874
    • Prinz, W.A.1
  • 52
    • 0017660232 scopus 로고
    • Translocation of phospholipids between the outer and inner membranes of Salmonella typhimurium
    • N.C. Jones, and M.J. Osborn Translocation of phospholipids between the outer and inner membranes of Salmonella typhimurium J. Biol. Chem. 252 1977 7405 7412
    • (1977) J. Biol. Chem. , vol.252 , pp. 7405-7412
    • Jones, N.C.1    Osborn, M.J.2
  • 53
    • 66049121818 scopus 로고    scopus 로고
    • An ABC transport system that maintains lipid asymmetry in the Gram-negative outer membrane
    • J.C. Malinverni, and T.J. Silhavy An ABC transport system that maintains lipid asymmetry in the Gram-negative outer membrane Proc. Natl. Acad. Sci. U.S.A. 106 2009 8009 8014
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8009-8014
    • Malinverni, J.C.1    Silhavy, T.J.2
  • 54
    • 69249101589 scopus 로고    scopus 로고
    • Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands
    • A.A. Lilly, J.M. Crane, and L.L. Randall Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands Protein Sci. 18 2009 1860 1868
    • (2009) Protein Sci. , vol.18 , pp. 1860-1868
    • Lilly, A.A.1    Crane, J.M.2    Randall, L.L.3
  • 55
    • 0141869958 scopus 로고    scopus 로고
    • Secretion of LamB-LacZ by the signal recognition particle pathway of Escherichia coli
    • C.W. Bowers, F. Lau, and T.J. Silhavy Secretion of LamB-LacZ by the signal recognition particle pathway of Escherichia coli J. Bacteriol. 185 2003 5697 5705
    • (2003) J. Bacteriol. , vol.185 , pp. 5697-5705
    • Bowers, C.W.1    Lau, F.2    Silhavy, T.J.3
  • 56
    • 0035853079 scopus 로고    scopus 로고
    • The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal
    • H.C. Lee, and H.D. Bernstein The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal Proc. Natl. Acad. Sci. U.S.A. 98 2001 3471 3476
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 3471-3476
    • Lee, H.C.1    Bernstein, H.D.2
  • 58
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in bacteria
    • [Electronic publication ahead of print]
    • S. Okuda, and H. Tokuda Lipoprotein sorting in bacteria Annu. Rev. Microbiol. 65 2011 [Electronic publication ahead of print]
    • (2011) Annu. Rev. Microbiol. , vol.65
    • Okuda, S.1    Tokuda, H.2
  • 59
    • 65249085615 scopus 로고    scopus 로고
    • Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB
    • S. Okuda, and H. Tokuda Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB Proc. Natl. Acad. Sci. U.S.A. 106 2009 5877 5882
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 5877-5882
    • Okuda, S.1    Tokuda, H.2
  • 60
    • 0141890241 scopus 로고    scopus 로고
    • Mechanism underlying the inner membrane retention of Escherichia coli lipoproteins caused by Lol avoidance signals
    • T. Hara Mechanism underlying the inner membrane retention of Escherichia coli lipoproteins caused by Lol avoidance signals J. Biol. Chem. 278 2003 40408 40414
    • (2003) J. Biol. Chem. , vol.278 , pp. 40408-40414
    • Hara, T.1
  • 61
    • 0032701349 scopus 로고    scopus 로고
    • Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection
    • A. Seydel, P. Gounon, and A.P. Pugsley Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection Mol. Microbiol. 34 1999 810 821
    • (1999) Mol. Microbiol. , vol.34 , pp. 810-821
    • Seydel, A.1    Gounon, P.2    Pugsley, A.P.3
  • 62
    • 0026572093 scopus 로고
    • Structural determinants in addition to the amino-terminal sorting sequence influence membrane localization of Escherichia coli lipoproteins
    • J.M. Gennity, H. Kim, and M. Inouye Structural determinants in addition to the amino-terminal sorting sequence influence membrane localization of Escherichia coli lipoproteins J. Bacteriol. 174 1992 2095 2101
    • (1992) J. Bacteriol. , vol.174 , pp. 2095-2101
    • Gennity, J.M.1    Kim, H.2    Inouye, M.3
  • 64
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • K.R. Hardie, S. Lory, and A.P. Pugsley Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein EMBO J. 15 1996 978 988
    • (1996) EMBO J. , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 66
    • 43949125856 scopus 로고    scopus 로고
    • The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon
    • R. Antonoaea, M. Fürst, K.-I. Nishiyama, and M. Müller The periplasmic chaperone PpiD interacts with secretory proteins exiting from the SecYEG translocon Biochemistry 47 2008 5649 5656
    • (2008) Biochemistry , vol.47 , pp. 5649-5656
    • Antonoaea, R.1    Fürst, M.2    Nishiyama, K.-I.3    Müller, M.4
  • 67
    • 0038105593 scopus 로고    scopus 로고
    • Skp, a molecular chaperone of Gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • U. Schäfer, K. Beck, and M. Müller Skp, a molecular chaperone of Gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins J. Biol. Chem. 274 1999 24567 24574
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schäfer, U.1    Beck, K.2    Müller, M.3
  • 68
    • 0035374452 scopus 로고    scopus 로고
    • The early interaction of the outer membrane protein PhoE with the periplasmic chaperone Skp occurs at the cytoplasmic membrane
    • N. Harms, G. Koningstein, W. Dontje, M. Muller, B. Oudega, J. Luirink, and H. de Cock The early interaction of the outer membrane protein PhoE with the periplasmic chaperone Skp occurs at the cytoplasmic membrane J. Biol. Chem. 276 2001 18804 18811
    • (2001) J. Biol. Chem. , vol.276 , pp. 18804-18811
    • Harms, N.1    Koningstein, G.2    Dontje, W.3    Muller, M.4    Oudega, B.5    Luirink, J.6    De Cock, H.7
  • 69
    • 33846234653 scopus 로고    scopus 로고
    • Kinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment
    • A.R. Ureta, R.G. Endres, N.S. Wingreen, and T.J. Silhavy Kinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment J. Bacteriol. 189 2007 446 454
    • (2007) J. Bacteriol. , vol.189 , pp. 446-454
    • Ureta, A.R.1    Endres, R.G.2    Wingreen, N.S.3    Silhavy, T.J.4
  • 70
    • 77955127606 scopus 로고    scopus 로고
    • Managing membrane stress: The phage shock protein (Psp) response, from molecular mechanisms to physiology
    • N. Joly, C. Engl, G. Jovanovic, M. Huvet, T. Toni, X. Sheng, M.P.H. Stumpf, and M. Buck Managing membrane stress: the phage shock protein (Psp) response, from molecular mechanisms to physiology FEMS Microbiol. Rev. 34 2010 797 827
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 797-827
    • Joly, N.1    Engl, C.2    Jovanovic, G.3    Huvet, M.4    Toni, T.5    Sheng, X.6    Stumpf, M.P.H.7    Buck, M.8
  • 71
    • 0025309069 scopus 로고
    • SurA, an Escherichia coli gene essential for survival in stationary phase
    • A. Tormo, M. Almiron, and R. Kolter surA, an Escherichia coli gene essential for survival in stationary phase J. Bacteriol. 172 1990 4339 4347
    • (1990) J. Bacteriol. , vol.172 , pp. 4339-4347
    • Tormo, A.1    Almiron, M.2    Kolter, R.3
  • 72
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
    • J.G. Sklar, T. Wu, D. Kahne, and T.J. Silhavy Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli Genes Dev. 21 2007 2473 2484
    • (2007) Genes Dev. , vol.21 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 73
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • S.W. Lazar, and R. Kolter SurA assists the folding of Escherichia coli outer membrane proteins J. Bacteriol. 178 1996 1770 1773
    • (1996) J. Bacteriol. , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 74
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • P.E. Rouviere, and C.A. Gross SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins Genes Dev. 10 1996 3170 3182
    • (1996) Genes Dev. , vol.10 , pp. 3170-3182
    • Rouviere, P.E.1    Gross, C.A.2
  • 75
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • D. Missiakas, J.M. Betton, and S. Raina New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH Mol. Microbiol. 21 1996 871 884
    • (1996) Mol. Microbiol. , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 76
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • S. Behrens, R. Maier, H. de Cock, F.X. Schmid, and C.A. Gross The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity EMBO J. 20 2001 285 294
    • (2001) EMBO J. , vol.20 , pp. 285-294
    • Behrens, S.1    Maier, R.2    De Cock, H.3    Schmid, F.X.4    Gross, C.A.5
  • 77
    • 2942622465 scopus 로고    scopus 로고
    • Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins
    • E. Bitto, and D.B. McKay Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins FEBS Lett. 568 2004 94 98
    • (2004) FEBS Lett. , vol.568 , pp. 94-98
    • Bitto, E.1    McKay, D.B.2
  • 78
    • 1542571983 scopus 로고    scopus 로고
    • The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins
    • E. Bitto, and D.B. McKay The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins J. Biol. Chem. 278 2003 49316 49322
    • (2003) J. Biol. Chem. , vol.278 , pp. 49316-49322
    • Bitto, E.1    McKay, D.B.2
  • 79
    • 21244447713 scopus 로고    scopus 로고
    • The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition
    • G. Hennecke, J. Nolte, R. Volkmer-Engert, J. Schneider-Mergener, and S. Behrens The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition J. Biol. Chem. 280 2005 23540 23548
    • (2005) J. Biol. Chem. , vol.280 , pp. 23540-23548
    • Hennecke, G.1    Nolte, J.2    Volkmer-Engert, R.3    Schneider-Mergener, J.4    Behrens, S.5
  • 80
    • 44949180774 scopus 로고    scopus 로고
    • The periplasmic peptidyl prolyl cis-trans isomerases PpiD and SurA have partially overlapping substrate specificities
    • K.H. Stymest, and P. Klappa The periplasmic peptidyl prolyl cis-trans isomerases PpiD and SurA have partially overlapping substrate specificities FEBS J. 275 2008 3470 3479
    • (2008) FEBS J. , vol.275 , pp. 3470-3479
    • Stymest, K.H.1    Klappa, P.2
  • 81
    • 0035824680 scopus 로고    scopus 로고
    • Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id essential and sufficient for peptide binding
    • H.M. Webb, L.W. Ruddock, R.J. Marchant, K. Jonas, and P. Klappa Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id essential and sufficient for peptide binding J. Biol. Chem. 276 2001 45622 45627
    • (2001) J. Biol. Chem. , vol.276 , pp. 45622-45627
    • Webb, H.M.1    Ruddock, L.W.2    Marchant, R.J.3    Jonas, K.4    Klappa, P.5
  • 82
    • 34548851967 scopus 로고    scopus 로고
    • The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues
    • X. Xu, S. Wang, Y.-X. Hu, and D.B. McKay The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues J. Mol. Biol. 373 2007 367 381
    • (2007) J. Mol. Biol. , vol.373 , pp. 367-381
    • Xu, X.1    Wang, S.2    Hu, Y.-X.3    McKay, D.B.4
  • 83
    • 0036849659 scopus 로고    scopus 로고
    • Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins
    • E. Bitto, and D.B. McKay Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins Structure 10 2002 1489 1498
    • (2002) Structure , vol.10 , pp. 1489-1498
    • Bitto, E.1    McKay, D.B.2
  • 84
    • 53749086601 scopus 로고    scopus 로고
    • Components of SurA required for outer membrane biogenesis in uropathogenic Escherichia coli
    • K.M. Watts, and D.A. Hunstad Components of SurA required for outer membrane biogenesis in uropathogenic Escherichia coli PLoS One 3 2008 e3359
    • (2008) PLoS One , vol.3 , pp. 3359
    • Watts, K.M.1    Hunstad, D.A.2
  • 85
    • 78751577599 scopus 로고    scopus 로고
    • The crystal structure of the leptospiral hypothetical protein LIC12922 reveals homology with the periplasmic chaperone SurA
    • P.O. Giuseppe, M.V. Atzingen, A.L.T.O. Nascimento, N.I.T. Zanchin, and B.G. Guimarães The crystal structure of the leptospiral hypothetical protein LIC12922 reveals homology with the periplasmic chaperone SurA J. Struct. Biol. 173 2011 312 322
    • (2011) J. Struct. Biol. , vol.173 , pp. 312-322
    • Giuseppe, P.O.1    Atzingen, M.V.2    Nascimento, A.L.T.O.3    Zanchin, N.I.T.4    Guimarães, B.G.5
  • 86
    • 66249114348 scopus 로고    scopus 로고
    • Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics
    • D. Vertommen, N. Ruiz, P. Leverrier, T.J. Silhavy, and J.-F. Collet Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics Proteomics 9 2009 2432 2443
    • (2009) Proteomics , vol.9 , pp. 2432-2443
    • Vertommen, D.1    Ruiz, N.2    Leverrier, P.3    Silhavy, T.J.4    Collet, J.-F.5
  • 87
    • 17444385981 scopus 로고    scopus 로고
    • Chemical conditionality: A genetic strategy to probe organelle assembly
    • N. Ruiz, B. Falcone, D. Kahne, and T.J. Silhavy Chemical conditionality: a genetic strategy to probe organelle assembly Cell 121 2005 307 317
    • (2005) Cell , vol.121 , pp. 307-317
    • Ruiz, N.1    Falcone, B.2    Kahne, D.3    Silhavy, T.J.4
  • 88
    • 0036046150 scopus 로고    scopus 로고
    • Imp/OstA is required for cell envelope biogenesis in Escherichia coli
    • M. Braun, and T.J. Silhavy Imp/OstA is required for cell envelope biogenesis in Escherichia coli Mol. Microbiol. 45 2002 1289 1302
    • (2002) Mol. Microbiol. , vol.45 , pp. 1289-1302
    • Braun, M.1    Silhavy, T.J.2
  • 89
    • 0015973774 scopus 로고
    • Protein composition of the outer membrane of Salmonella typhimurium: Effect of lipopolysaccharide mutations
    • G.F. Ames, E.N. Spudich, and H. Nikaido Protein composition of the outer membrane of Salmonella typhimurium: effect of lipopolysaccharide mutations J. Bacteriol. 117 1974 406 416
    • (1974) J. Bacteriol. , vol.117 , pp. 406-416
    • Ames, G.F.1    Spudich, E.N.2    Nikaido, H.3
  • 90
    • 0015969864 scopus 로고
    • Alterations in the outer membrane of the cell envelope of heptose-deficient mutants of Escherichia coli
    • J. Koplow, and H. Goldfine Alterations in the outer membrane of the cell envelope of heptose-deficient mutants of Escherichia coli J. Bacteriol. 117 1974 527 543
    • (1974) J. Bacteriol. , vol.117 , pp. 527-543
    • Koplow, J.1    Goldfine, H.2
  • 91
    • 0028297759 scopus 로고
    • Assembly of LamB and OmpF in deep rough lipopolysaccharide mutants of Escherichia coli K-12
    • M.W. Laird, A.W. Kloser, and R. Misra Assembly of LamB and OmpF in deep rough lipopolysaccharide mutants of Escherichia coli K-12 J. Bacteriol. 176 1994 2259 2264
    • (1994) J. Bacteriol. , vol.176 , pp. 2259-2264
    • Laird, M.W.1    Kloser, A.W.2    Misra, R.3
  • 92
    • 0024119777 scopus 로고
    • The assembly of the major outer membrane protein OmpF of Escherichia coli depends on lipid synthesis
    • J.M. Bolla, C. Lazdunski, and J.M. Pagès The assembly of the major outer membrane protein OmpF of Escherichia coli depends on lipid synthesis EMBO J. 7 1988 3595 3599
    • (1988) EMBO J. , vol.7 , pp. 3595-3599
    • Bolla, J.M.1    Lazdunski, C.2    Pagès, J.M.3
  • 93
    • 0037516675 scopus 로고    scopus 로고
    • N-Hexane sensitivity of Escherichia coli due to low expression of imp/ostA encoding an 87 kDa minor protein associated with the outer membrane
    • S. Abe, T. Okutsu, H. Nakajima, N. Kakuda, I. Ohtsu, and R. Aono n-Hexane sensitivity of Escherichia coli due to low expression of imp/ostA encoding an 87 kDa minor protein associated with the outer membrane Microbiology (Reading, Engl) 149 2003 1265 1273
    • (2003) Microbiology (Reading, Engl) , vol.149 , pp. 1265-1273
    • Abe, S.1    Okutsu, T.2    Nakajima, H.3    Kakuda, N.4    Ohtsu, I.5    Aono, R.6
  • 94
    • 0024690869 scopus 로고
    • Identification and characterization of a new gene of Escherichia coli K-12 involved in outer membrane permeability
    • B.A. Sampson, R. Misra, and S.A. Benson Identification and characterization of a new gene of Escherichia coli K-12 involved in outer membrane permeability Genetics 122 1989 491 501
    • (1989) Genetics , vol.122 , pp. 491-501
    • Sampson, B.A.1    Misra, R.2    Benson, S.A.3
  • 95
    • 77952363712 scopus 로고    scopus 로고
    • Reconstitution of outer membrane protein assembly from purified components
    • C.L. Hagan, S. Kim, and D. Kahne Reconstitution of outer membrane protein assembly from purified components Science 328 2010 890 892
    • (2010) Science , vol.328 , pp. 890-892
    • Hagan, C.L.1    Kim, S.2    Kahne, D.3
  • 96
    • 27744565064 scopus 로고    scopus 로고
    • Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli
    • S.S. Justice, D.A. Hunstad, J.R. Harper, A.R. Duguay, J.S. Pinkner, J. Bann, C. Frieden, T.J. Silhavy, and S.J. Hultgren Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli J. Bacteriol. 187 2005 7680 7686
    • (2005) J. Bacteriol. , vol.187 , pp. 7680-7686
    • Justice, S.S.1    Hunstad, D.A.2    Harper, J.R.3    Duguay, A.R.4    Pinkner, J.S.5    Bann, J.6    Frieden, C.7    Silhavy, T.J.8    Hultgren, S.J.9
  • 97
    • 73149118024 scopus 로고    scopus 로고
    • Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane
    • R. Ieva, and H.D. Bernstein Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane Proc. Natl. Acad. Sci. U.S.A. 106 2009 19120 19125
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 19120-19125
    • Ieva, R.1    Bernstein, H.D.2
  • 98
    • 70350470007 scopus 로고    scopus 로고
    • Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae
    • F. Ruiz-Perez, I.R. Henderson, D.L. Leyton, A.E. Rossiter, Y. Zhang, and J.P. Nataro Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae J. Bacteriol. 191 2009 6571 6583
    • (2009) J. Bacteriol. , vol.191 , pp. 6571-6583
    • Ruiz-Perez, F.1    Henderson, I.R.2    Leyton, D.L.3    Rossiter, A.E.4    Zhang, Y.5    Nataro, J.P.6
  • 100
    • 34547643207 scopus 로고    scopus 로고
    • IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA
    • G.E. Purdy, C.R. Fisher, and S.M. Payne IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA J. Bacteriol. 189 2007 5566 5573
    • (2007) J. Bacteriol. , vol.189 , pp. 5566-5573
    • Purdy, G.E.1    Fisher, C.R.2    Payne, S.M.3
  • 101
    • 67749127364 scopus 로고    scopus 로고
    • Role of periplasmic chaperones and BamA (YaeT/Omp85) in folding and secretion of intimin from enteropathogenic Escherichia coli strains
    • G. Bodelon, E. Marin, and L.A. Fernandez Role of periplasmic chaperones and BamA (YaeT/Omp85) in folding and secretion of intimin from enteropathogenic Escherichia coli strains J. Bacteriol. 191 2009 5169 5179
    • (2009) J. Bacteriol. , vol.191 , pp. 5169-5179
    • Bodelon, G.1    Marin, E.2    Fernandez, L.A.3
  • 103
    • 0024258616 scopus 로고
    • Identity of the 17-kilodalton protein, a DNA-binding protein from Escherichia coli, and the firA gene product
    • R. Aasland, J. Coleman, A.L. Holck, C.L. Smith, C.R. Raetz, and K. Kleppe Identity of the 17-kilodalton protein, a DNA-binding protein from Escherichia coli, and the firA gene product J. Bacteriol. 170 1988 5916 5918
    • (1988) J. Bacteriol. , vol.170 , pp. 5916-5918
    • Aasland, R.1    Coleman, J.2    Holck, A.L.3    Smith, C.L.4    Raetz, C.R.5    Kleppe, K.6
  • 104
    • 0025041015 scopus 로고
    • A protein with sequence identity to Skp (FirA) supports protein translocation into plasma membrane vesicles of Escherichia coli
    • B.M. Thome, H.K. Hoffschulte, E. Schiltz, and M. Muller A protein with sequence identity to Skp (FirA) supports protein translocation into plasma membrane vesicles of Escherichia coli FEBS Lett. 269 1990 113 116
    • (1990) FEBS Lett. , vol.269 , pp. 113-116
    • Thome, B.M.1    Hoffschulte, H.K.2    Schiltz, E.3    Muller, M.4
  • 105
    • 0026041449 scopus 로고
    • Skp is a periplasmic Escherichia coli protein requiring SecA and SecY for export
    • B.M. Thome, and M. Muller Skp is a periplasmic Escherichia coli protein requiring SecA and SecY for export Mol. Microbiol. 5 1991 2815 2821
    • (1991) Mol. Microbiol. , vol.5 , pp. 2815-2821
    • Thome, B.M.1    Muller, M.2
  • 106
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • R. Chen, and U. Henning A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins Mol. Microbiol. 19 1996 1287 1294
    • (1996) Mol. Microbiol. , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 107
    • 0035161025 scopus 로고    scopus 로고
    • Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
    • A.E. Rizzitello, J.R. Harper, and T.J. Silhavy Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli J. Bacteriol. 183 2001 6794 6800
    • (2001) J. Bacteriol. , vol.183 , pp. 6794-6800
    • Rizzitello, A.E.1    Harper, J.R.2    Silhavy, T.J.3
  • 108
    • 79952789687 scopus 로고    scopus 로고
    • Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis
    • E.B. Volokhina, J. Grijpstra, M. Stork, I. Schilders, J. Tommassen, and M.P. Bos Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis J. Bacteriol. 193 2011 1612 1621
    • (2011) J. Bacteriol. , vol.193 , pp. 1612-1621
    • Volokhina, E.B.1    Grijpstra, J.2    Stork, M.3    Schilders, I.4    Tommassen, J.5    Bos, M.P.6
  • 109
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • T.A. Walton, and M.C. Sousa Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation Mol. Cell 15 2004 367 374
    • (2004) Mol. Cell , vol.15 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2
  • 110
    • 4744373535 scopus 로고    scopus 로고
    • Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture
    • I.P. Korndörfer, M.K. Dommel, and A. Skerra Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture Nat. Struct. Mol. Biol. 11 2004 1015 1020
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1015-1020
    • Korndörfer, I.P.1    Dommel, M.K.2    Skerra, A.3
  • 111
    • 29544436323 scopus 로고    scopus 로고
    • Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller
    • C.T. Webb, M.A. Gorman, M. Lazarou, M.T. Ryan, and J.M. Gulbis Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller Mol. Cell 21 2006 123 133
    • (2006) Mol. Cell , vol.21 , pp. 123-133
    • Webb, C.T.1    Gorman, M.A.2    Lazarou, M.3    Ryan, M.T.4    Gulbis, J.M.5
  • 112
    • 35348966245 scopus 로고    scopus 로고
    • The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions
    • J. Qu, C. Mayer, S. Behrens, O. Holst, and J.H. Kleinschmidt The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions J. Mol. Biol. 374 2007 91 105
    • (2007) J. Mol. Biol. , vol.374 , pp. 91-105
    • Qu, J.1    Mayer, C.2    Behrens, S.3    Holst, O.4    Kleinschmidt, J.H.5
  • 113
    • 66649116274 scopus 로고    scopus 로고
    • Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study
    • J. Qu, S. Behrens-Kneip, O. Holst, and J.H. Kleinschmidt Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp. A site-directed fluorescence study Biochemistry 48 2009 4926 4936
    • (2009) Biochemistry , vol.48 , pp. 4926-4936
    • Qu, J.1    Behrens-Kneip, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 114
    • 60549101514 scopus 로고    scopus 로고
    • The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains
    • T.A. Walton, C.M. Sandoval, C.A. Fowler, A. Pardi, and M.C. Sousa The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains Proc. Natl. Acad. Sci. U.S.A. 106 2009 1772 1777
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 1772-1777
    • Walton, T.A.1    Sandoval, C.M.2    Fowler, C.A.3    Pardi, A.4    Sousa, M.C.5
  • 115
    • 57649242773 scopus 로고    scopus 로고
    • Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp
    • S. Jarchow, C. Lück, A. Görg, and A. Skerra Identification of potential substrate proteins for the periplasmic Escherichia coli chaperone Skp Proteomics 8 2008 4987 4994
    • (2008) Proteomics , vol.8 , pp. 4987-4994
    • Jarchow, S.1    Lück, C.2    Görg, A.3    Skerra, A.4
  • 116
    • 0037984384 scopus 로고    scopus 로고
    • Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide
    • P.V. Bulieris, S. Behrens, O. Holst, and J.H. Kleinschmidt Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide J. Biol. Chem. 278 2003 9092 9099
    • (2003) J. Biol. Chem. , vol.278 , pp. 9092-9099
    • Bulieris, P.V.1    Behrens, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 117
    • 60649107938 scopus 로고    scopus 로고
    • Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri
    • J.K. Wagner, J.E. Heindl, A.N. Gray, S. Jain, and M.B. Goldberg Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri J. Bacteriol. 191 2009 815 821
    • (2009) J. Bacteriol. , vol.191 , pp. 815-821
    • Wagner, J.K.1    Heindl, J.E.2    Gray, A.N.3    Jain, S.4    Goldberg, M.B.5
  • 119
    • 0032527831 scopus 로고    scopus 로고
    • A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
    • C. Dartigalongue, and S. Raina A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli EMBO J. 17 1998 3968 3980
    • (1998) EMBO J. , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 120
    • 77957135569 scopus 로고    scopus 로고
    • PpiD is a player in the network of periplasmic chaperones in Escherichia coli
    • Y. Matern, B. Barion, and S. Behrens-Kneip PpiD is a player in the network of periplasmic chaperones in Escherichia coli BMC Microbiol. 10 2010 251
    • (2010) BMC Microbiol. , vol.10 , pp. 251
    • Matern, Y.1    Barion, B.2    Behrens-Kneip, S.3
  • 121
    • 75149136165 scopus 로고    scopus 로고
    • The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity
    • U. Weininger, R.P. Jakob, M. Kovermann, J. Balbach, and F.X. Schmid The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity Protein Sci. 19 2010 6 18
    • (2010) Protein Sci. , vol.19 , pp. 6-18
    • Weininger, U.1    Jakob, R.P.2    Kovermann, M.3    Balbach, J.4    Schmid, F.X.5
  • 122
    • 0031024992 scopus 로고    scopus 로고
    • Decreased intracellular survival of an fkpA mutant of Salmonella typhimurium Copenhagen
    • S.M. Horne, T.J. Kottom, L.K. Nolan, and K.D. Young Decreased intracellular survival of an fkpA mutant of Salmonella typhimurium Copenhagen Infect. Immun. 65 1997 806 810
    • (1997) Infect. Immun. , vol.65 , pp. 806-810
    • Horne, S.M.1    Kottom, T.J.2    Nolan, L.K.3    Young, K.D.4
  • 123
    • 0346366809 scopus 로고    scopus 로고
    • Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
    • F.A. Saul, J.-P. Arié, B. Vulliez-le Normand, R. Kahn, J.-M. Betton, and G.A. Bentley Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity J. Mol. Biol. 335 2004 595 608
    • (2004) J. Mol. Biol. , vol.335 , pp. 595-608
    • Saul, F.A.1    Arié, J.-P.2    Vulliez-Le Normand, B.3    Kahn, R.4    Betton, J.-M.5    Bentley, G.A.6
  • 124
    • 0039423955 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines
    • H. Bothmann, and A. Pluckthun The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines J. Biol. Chem. 275 2000 17100 17105
    • (2000) J. Biol. Chem. , vol.275 , pp. 17100-17105
    • Bothmann, H.1    Pluckthun, A.2
  • 125
    • 0038831330 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro
    • K. Ramm, and A. Plückthun The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro J. Biol. Chem. 275 2000 17106 17113
    • (2000) J. Biol. Chem. , vol.275 , pp. 17106-17113
    • Ramm, K.1    Plückthun, A.2
  • 126
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • J.P. Arie, N. Sassoon, and J.M. Betton Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli Mol. Microbiol. 39 2001 199 210
    • (2001) Mol. Microbiol. , vol.39 , pp. 199-210
    • Arie, J.P.1    Sassoon, N.2    Betton, J.M.3
  • 127
    • 47749139311 scopus 로고    scopus 로고
    • Periplasmic chaperone FkpA is essential for imported colicin M toxicity
    • J. Hullmann, S.I. Patzer, C. Römer, K. Hantke, and V. Braun Periplasmic chaperone FkpA is essential for imported colicin M toxicity Mol. Microbiol. 69 2008 926 937
    • (2008) Mol. Microbiol. , vol.69 , pp. 926-937
    • Hullmann, J.1    Patzer, S.I.2    Römer, C.3    Hantke, K.4    Braun, V.5
  • 129
    • 0031024992 scopus 로고    scopus 로고
    • Decreased intracellular survival of an fkpA mutant of Salmonella typhimurium Copenhagen
    • S.M. Horne, T.J. Kottom, L.K. Nolan, and K.D. Young Decreased intracellular survival of an fkpA mutant of Salmonella typhimurium Copenhagen Infect. Immun. 65 1997 806 810
    • (1997) Infect. Immun. , vol.65 , pp. 806-810
    • Horne, S.M.1    Kottom, T.J.2    Nolan, L.K.3    Young, K.D.4
  • 130
    • 0028999723 scopus 로고
    • Secretion by Trypanosoma cruzi of a peptidyl-prolyl cis-trans isomerase involved in cell infection
    • A. Moro, F. Ruiz-Cabello, A. Fernández-Cano, R.P. Stock, and A. González Secretion by Trypanosoma cruzi of a peptidyl-prolyl cis-trans isomerase involved in cell infection EMBO J. 14 1995 2483 2490
    • (1995) EMBO J. , vol.14 , pp. 2483-2490
    • Moro, A.1    Ruiz-Cabello, F.2    Fernández-Cano, A.3    Stock, R.P.4    González, A.5
  • 131
    • 0041823295 scopus 로고    scopus 로고
    • Role of periplasmic peptidylprolyl isomerases in Salmonella enterica serovar Typhimurium virulence
    • S. Humphreys, G. Rowley, A. Stevenson, W.J. Kenyon, M.P. Spector, and M. Roberts Role of periplasmic peptidylprolyl isomerases in Salmonella enterica serovar Typhimurium virulence Infect. Immun. 71 2003 5386 5388
    • (2003) Infect. Immun. , vol.71 , pp. 5386-5388
    • Humphreys, S.1    Rowley, G.2    Stevenson, A.3    Kenyon, W.J.4    Spector, M.P.5    Roberts, M.6
  • 132
    • 79953219089 scopus 로고    scopus 로고
    • Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone
    • S. Helbig, S.I. Patzer, C. Schiene-Fischer, K. Zeth, and V. Braun Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone J. Biol. Chem. 286 2011 6280 6290
    • (2011) J. Biol. Chem. , vol.286 , pp. 6280-6290
    • Helbig, S.1    Patzer, S.I.2    Schiene-Fischer, C.3    Zeth, K.4    Braun, V.5
  • 133
    • 77957678381 scopus 로고    scopus 로고
    • Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein
    • F. Ruiz-Perez, I.R. Henderson, and J.P. Nataro Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein Gut Microbes 1 2010 339 344
    • (2010) Gut Microbes , vol.1 , pp. 339-344
    • Ruiz-Perez, F.1    Henderson, I.R.2    Nataro, J.P.3
  • 134
    • 0032432109 scopus 로고    scopus 로고
    • Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli
    • P.N. Danese, and T.J. Silhavy Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli Annu. Rev. Genet. 32 1998 59 94
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 59-94
    • Danese, P.N.1    Silhavy, T.J.2
  • 135
    • 22144495426 scopus 로고    scopus 로고
    • Interactions between folding factors and bacterial outer membrane proteins
    • J.E. Mogensen, and D.E. Otzen Interactions between folding factors and bacterial outer membrane proteins Mol. Microbiol. 57 2005 326 346
    • (2005) Mol. Microbiol. , vol.57 , pp. 326-346
    • Mogensen, J.E.1    Otzen, D.E.2
  • 136
    • 0030992719 scopus 로고    scopus 로고
    • Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system
    • J. Pogliano, A.S. Lynch, D. Belin, E.C. Lin, and J. Beckwith Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system Genes Dev. 11 1997 1169 1182
    • (1997) Genes Dev. , vol.11 , pp. 1169-1182
    • Pogliano, J.1    Lynch, A.S.2    Belin, D.3    Lin, E.C.4    Beckwith, J.5
  • 138
    • 67649205489 scopus 로고    scopus 로고
    • Assemblies of DegP underlie its dual chaperone and protease function
    • O. Subrini, and J.-M. Betton Assemblies of DegP underlie its dual chaperone and protease function FEMS Microbiol. Lett. 296 2009 143 148
    • (2009) FEMS Microbiol. Lett. , vol.296 , pp. 143-148
    • Subrini, O.1    Betton, J.-M.2
  • 139
    • 77954384306 scopus 로고    scopus 로고
    • HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
    • T. Krojer, J. Sawa, R. Huber, and T. Clausen HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues Nat. Struct. Mol. Biol. 17 2010 844 852
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 844-852
    • Krojer, T.1    Sawa, J.2    Huber, R.3    Clausen, T.4
  • 140
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • T. Krojer, J. Sawa, E. Schäfer, H.R. Saibil, M. Ehrmann, and T. Clausen Structural basis for the regulated protease and chaperone function of DegP Nature 453 2008 885 890
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schäfer, E.3    Saibil, H.R.4    Ehrmann, M.5    Clausen, T.6
  • 141
    • 0037214416 scopus 로고    scopus 로고
    • Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture
    • M. CastilloKeller, and R. Misra Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture J. Bacteriol. 185 2003 148 154
    • (2003) J. Bacteriol. , vol.185 , pp. 148-154
    • Castillokeller, M.1    Misra, R.2
  • 142
    • 0033870158 scopus 로고    scopus 로고
    • Overexpression of protease-deficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background
    • R. Misra, M. CastilloKeller, and M. Deng Overexpression of protease-deficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background J. Bacteriol. 182 2000 4882 4888
    • (2000) J. Bacteriol. , vol.182 , pp. 4882-4888
    • Misra, R.1    Castillokeller, M.2    Deng, M.3
  • 143
    • 0031580211 scopus 로고    scopus 로고
    • Role of the carboxy-terminal phenylalanine in the biogenesis of outer membrane protein PhoE of Escherichia coli K-12
    • H. de Cock, M. Struyvé, M. Kleerebezem, T. van der Krift, and J. Tommassen Role of the carboxy-terminal phenylalanine in the biogenesis of outer membrane protein PhoE of Escherichia coli K-12 J. Mol. Biol. 269 1997 473 478
    • (1997) J. Mol. Biol. , vol.269 , pp. 473-478
    • De Cock, H.1    Struyvé, M.2    Kleerebezem, M.3    Van Der Krift, T.4    Tommassen, J.5
  • 144
    • 0025976068 scopus 로고
    • Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein
    • M. Struyvé, M. Moons, and J. Tommassen Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein J. Mol. Biol. 218 1991 141 148
    • (1991) J. Mol. Biol. , vol.218 , pp. 141-148
    • Struyvé, M.1    Moons, M.2    Tommassen, J.3
  • 145
    • 0010461565 scopus 로고    scopus 로고
    • The assembly pathway of outer membrane protein PhoE of Escherichia coli
    • C. Jansen, M. Heutink, J. Tommassen, and H. de Cock The assembly pathway of outer membrane protein PhoE of Escherichia coli Eur. J. Biochem. 267 2000 3792 3800
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3792-3800
    • Jansen, C.1    Heutink, M.2    Tommassen, J.3    De Cock, H.4
  • 147
    • 77956634838 scopus 로고    scopus 로고
    • Porins in prokaryotes and eukaryotes: Common themes and variations
    • K. Zeth, and M. Thein Porins in prokaryotes and eukaryotes: common themes and variations Biochem. J. 431 2010 13 22
    • (2010) Biochem. J. , vol.431 , pp. 13-22
    • Zeth, K.1    Thein, M.2
  • 148
    • 0033613822 scopus 로고    scopus 로고
    • Membrane assembly of the Escherichia coli outer membrane protein OmpA: Exploring sequence constraints on transmembrane beta-strands
    • R. Koebnik Membrane assembly of the Escherichia coli outer membrane protein OmpA: exploring sequence constraints on transmembrane beta-strands J. Mol. Biol. 285 1999 1801 1810
    • (1999) J. Mol. Biol. , vol.285 , pp. 1801-1810
    • Koebnik, R.1
  • 149
    • 0030010702 scopus 로고    scopus 로고
    • In vivo membrane assembly of split variants of the E. coli outer membrane protein OmpA
    • R. Koebnik In vivo membrane assembly of split variants of the E. coli outer membrane protein OmpA EMBO J. 15 1996 3529 3537
    • (1996) EMBO J. , vol.15 , pp. 3529-3537
    • Koebnik, R.1
  • 150
    • 79751537491 scopus 로고    scopus 로고
    • Lipid-binding surfaces of membrane proteins: Evidence from evolutionary and structural analysis
    • L. Adamian, H. Naveed, and J. Liang Lipid-binding surfaces of membrane proteins: evidence from evolutionary and structural analysis Biochim. Biophys. Acta 1808 2011 1092 1102
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 1092-1102
    • Adamian, L.1    Naveed, H.2    Liang, J.3
  • 151
    • 69149083388 scopus 로고    scopus 로고
    • Predicting weakly stable regions, oligomerization state, and protein-protein interfaces in transmembrane domains of outer membrane proteins
    • H. Naveed, R. Jackups, and J. Liang Predicting weakly stable regions, oligomerization state, and protein-protein interfaces in transmembrane domains of outer membrane proteins Proc. Natl. Acad. Sci. U.S.A. 106 2009 12735 12740
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 12735-12740
    • Naveed, H.1    Jackups, R.2    Liang, J.3
  • 152
    • 0042878499 scopus 로고    scopus 로고
    • Membrane protein folding on the example of outer membrane protein A of Escherichia coli
    • J.H. Kleinschmidt Membrane protein folding on the example of outer membrane protein A of Escherichia coli Cell. Mol. Life Sci. 60 2003 1547 1558
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1547-1558
    • Kleinschmidt, J.H.1
  • 153
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • I. Gentle, K. Gabriel, P. Beech, R. Waller, and T. Lithgow The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria J. Cell Biol. 164 2004 19 24
    • (2004) J. Cell Biol. , vol.164 , pp. 19-24
    • Gentle, I.1    Gabriel, K.2    Beech, P.3    Waller, R.4    Lithgow, T.5
  • 154
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • R. Voulhoux, M.P. Bos, J. Geurtsen, M. Mols, and J. Tommassen Role of a highly conserved bacterial protein in outer membrane protein assembly Science 299 2003 262 265
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 155
    • 77952894531 scopus 로고    scopus 로고
    • Omp85 from the thermophilic cyanobacterium Thermosynechococcus elongatus differs from proteobacterial Omp85 in structure and domain composition
    • T. Arnold, K. Zeth, and D. Linke Omp85 from the thermophilic cyanobacterium Thermosynechococcus elongatus differs from proteobacterial Omp85 in structure and domain composition J. Biol. Chem. 285 2010 18003 18015
    • (2010) J. Biol. Chem. , vol.285 , pp. 18003-18015
    • Arnold, T.1    Zeth, K.2    Linke, D.3
  • 158
    • 78651374569 scopus 로고    scopus 로고
    • Omp85 in eukaryotic systems: One protein family with distinct functions
    • E. Schleiff, U.G. Maier, and T. Becker Omp85 in eukaryotic systems: one protein family with distinct functions Biol. Chem. 392 2011 21 27
    • (2011) Biol. Chem. , vol.392 , pp. 21-27
    • Schleiff, E.1    Maier, U.G.2    Becker, T.3
  • 161
    • 34548139422 scopus 로고    scopus 로고
    • Structure and function of an essential component of the outer membrane protein assembly machine
    • S. Kim, J.C. Malinverni, P. Sliz, T.J. Silhavy, S.C. Harrison, and D. Kahne Structure and function of an essential component of the outer membrane protein assembly machine Science 317 2007 961 964
    • (2007) Science , vol.317 , pp. 961-964
    • Kim, S.1    Malinverni, J.C.2    Sliz, P.3    Silhavy, T.J.4    Harrison, S.C.5    Kahne, D.6
  • 162
    • 34547512065 scopus 로고    scopus 로고
    • Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli
    • J.G. Sklar, T. Wu, L.S. Gronenberg, J.C. Malinverni, D. Kahne, and T.J. Silhavy Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 104 2007 6400 6405
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 6400-6405
    • Sklar, J.G.1    Wu, T.2    Gronenberg, L.S.3    Malinverni, J.C.4    Kahne, D.5    Silhavy, T.J.6
  • 163
    • 70350434092 scopus 로고    scopus 로고
    • The beta-barrel outer membrane protein assembly complex of Neisseria meningitidis
    • E.B. Volokhina, F. Beckers, J. Tommassen, and M.P. Bos The beta-barrel outer membrane protein assembly complex of Neisseria meningitidis J. Bacteriol. 191 2009 7074 7085
    • (2009) J. Bacteriol. , vol.191 , pp. 7074-7085
    • Volokhina, E.B.1    Beckers, F.2    Tommassen, J.3    Bos, M.P.4
  • 164
    • 28244436432 scopus 로고    scopus 로고
    • Molecular architecture and function of the Omp85 family of proteins
    • I.E. Gentle, L. Burri, and T. Lithgow Molecular architecture and function of the Omp85 family of proteins Mol. Microbiol. 58 2005 1216 1225
    • (2005) Mol. Microbiol. , vol.58 , pp. 1216-1225
    • Gentle, I.E.1    Burri, L.2    Lithgow, T.3
  • 165
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: A conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins
    • L. Sánchez-Pulido, D. Devos, S. Genevrois, M. Vicente, and A. Valencia POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins Trends Biochem. Sci. 28 2003 523 526
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 523-526
    • Sánchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vicente, M.4    Valencia, A.5
  • 166
    • 36749048640 scopus 로고    scopus 로고
    • Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain
    • M.P. Bos, V. Robert, and J. Tommassen Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain EMBO Rep. 8 2007 1149 1154
    • (2007) EMBO Rep. , vol.8 , pp. 1149-1154
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 167
    • 3042554408 scopus 로고    scopus 로고
    • Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface
    • M.P. Bos, B. Tefsen, J. Geurtsen, and J. Tommassen Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface Proc. Natl. Acad. Sci. U.S.A. 101 2004 9417 9422
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 9417-9422
    • Bos, M.P.1    Tefsen, B.2    Geurtsen, J.3    Tommassen, J.4
  • 169
    • 33749593869 scopus 로고    scopus 로고
    • Differential effects of yfgL mutation on Escherichia coli outer membrane proteins and lipopolysaccharide
    • E.S. Charlson, J.N. Werner, and R. Misra Differential effects of yfgL mutation on Escherichia coli outer membrane proteins and lipopolysaccharide J. Bacteriol. 188 2006 7186 7194
    • (2006) J. Bacteriol. , vol.188 , pp. 7186-7194
    • Charlson, E.S.1    Werner, J.N.2    Misra, R.3
  • 170
    • 39749086276 scopus 로고    scopus 로고
    • Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry
    • P. Vuong, D. Bennion, J. Mantei, D. Frost, and R. Misra Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry J. Bacteriol. 190 2008 1507 1517
    • (2008) J. Bacteriol. , vol.190 , pp. 1507-1517
    • Vuong, P.1    Bennion, D.2    Mantei, J.3    Frost, D.4    Misra, R.5
  • 171
    • 77956153485 scopus 로고    scopus 로고
    • Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli
    • D. Bennion, E.S. Charlson, E. Coon, and R. Misra Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli Mol. Microbiol. 77 2010 1153 1171
    • (2010) Mol. Microbiol. , vol.77 , pp. 1153-1171
    • Bennion, D.1    Charlson, E.S.2    Coon, E.3    Misra, R.4
  • 172
    • 79952311132 scopus 로고    scopus 로고
    • The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex
    • N. Noinaj, J.W. Fairman, and S.K. Buchanan The crystal structure of BamB
    • (2011) J. Mol. Biol. , vol.407 , pp. 248-260
    • Noinaj, N.1    Fairman, J.W.2    Buchanan, S.K.3
  • 173
    • 57049171923 scopus 로고    scopus 로고
    • Crystal structure of YaeT: Conformational flexibility and substrate recognition
    • P.Z. Gatzeva-Topalova, T.A. Walton, and M.C. Sousa Crystal structure of YaeT: conformational flexibility and substrate recognition Structure 16 2008 1873 1881
    • (2008) Structure , vol.16 , pp. 1873-1881
    • Gatzeva-Topalova, P.Z.1    Walton, T.A.2    Sousa, M.C.3
  • 174
  • 175
    • 69849099037 scopus 로고    scopus 로고
    • The orientation of a tandem POTRA domain pair, of the beta-barrel assembly protein BamA, determined by PELDOR spectroscopy
    • R. Ward, M. Zoltner, L. Beer, H. El Mkami, I.R. Henderson, T. Palmer, and D.G. Norman The orientation of a tandem POTRA domain pair, of the beta-barrel assembly protein BamA, determined by PELDOR spectroscopy Structure 17 2009 1187 1194
    • (2009) Structure , vol.17 , pp. 1187-1194
    • Ward, R.1    Zoltner, M.2    Beer, L.3    El Mkami, H.4    Henderson, I.R.5    Palmer, T.6    Norman, D.G.7
  • 176
    • 78149430938 scopus 로고    scopus 로고
    • Structure and flexibility of the complete periplasmic domain of BamA: The protein insertion machine of the outer membrane
    • P.Z. Gatzeva-Topalova, L.R. Warner, A. Pardi, and M.C. Sousa Structure and flexibility of the complete periplasmic domain of BamA: the protein insertion machine of the outer membrane Structure 18 2010 1492 1501
    • (2010) Structure , vol.18 , pp. 1492-1501
    • Gatzeva-Topalova, P.Z.1    Warner, L.R.2    Pardi, A.3    Sousa, M.C.4
  • 178
    • 34547534673 scopus 로고    scopus 로고
    • Probing the barrier function of the outer membrane with chemical conditionality
    • N. Ruiz, T. Wu, D. Kahne, and T.J. Silhavy Probing the barrier function of the outer membrane with chemical conditionality ACS Chem. Biol. 1 2006 385 395
    • (2006) ACS Chem. Biol. , vol.1 , pp. 385-395
    • Ruiz, N.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 181
    • 78049291824 scopus 로고    scopus 로고
    • Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily
    • A.-S. Delattre, B. Clantin, N. Saint, C. Locht, V. Villeret, and F. Jacob-Dubuisson Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily FEBS J. 277 2010 4755 4765
    • (2010) FEBS J. , vol.277 , pp. 4755-4765
    • Delattre, A.-S.1    Clantin, B.2    Saint, N.3    Locht, C.4    Villeret, V.5    Jacob-Dubuisson, F.6
  • 182
    • 79960974503 scopus 로고    scopus 로고
    • Structural basis of outer membrane protein biogenesis in bacteria
    • R. Albrecht, and K. Zeth Structural basis of outer membrane protein biogenesis in bacteria J. Biol. Chem. 286 31 2011 27792 27803
    • (2011) J. Biol. Chem. , vol.286 , Issue.31 , pp. 27792-27803
    • Albrecht, R.1    Zeth, K.2
  • 183
    • 79951769354 scopus 로고    scopus 로고
    • Augmenting β-augmentation: Structural basis of how BamB binds BamA and may support folding of outer membrane proteins
    • A. Heuck, A. Schleiffer, and T. Clausen Augmenting β-augmentation: structural basis of how BamB binds BamA and may support folding of outer membrane proteins J. Mol. Biol. 406 2011 659 666
    • (2011) J. Mol. Biol. , vol.406 , pp. 659-666
    • Heuck, A.1    Schleiffer, A.2    Clausen, T.3
  • 184
    • 79951772443 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli BamB, a lipoprotein component of the β-barrel assembly machinery complex
    • K.H. Kim, and M. Paetzel Crystal structure of Escherichia coli BamB, a lipoprotein component of the β-barrel assembly machinery complex J. Mol. Biol. 406 2011 667 678
    • (2011) J. Mol. Biol. , vol.406 , pp. 667-678
    • Kim, K.H.1    Paetzel, M.2
  • 185
    • 79960698669 scopus 로고    scopus 로고
    • Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set
    • L.R. Warner, K. Varga, O.F. Lange, S.L. Baker, D. Baker, M.C. Sousa, and A. Pardi Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set J. Mol. Biol. 411 1 2011 83 95
    • (2011) J. Mol. Biol. , vol.411 , Issue.1 , pp. 83-95
    • Warner, L.R.1    Varga, K.2    Lange, O.F.3    Baker, S.L.4    Baker, D.5    Sousa, M.C.6    Pardi, A.7
  • 186
    • 79956148245 scopus 로고    scopus 로고
    • Crystal structure of BamD. an essential component of the β-barrel assembly machinery of Gram negative bacteria
    • C.M. Sandoval, S.L. Baker, K. Jansen, S.I. Metzner, and M.C. Sousa Crystal structure of BamD. an essential component of the β-barrel assembly machinery of Gram negative bacteria J. Mol. Biol. 409 3 2011 348 357
    • (2011) J. Mol. Biol. , vol.409 , Issue.3 , pp. 348-357
    • Sandoval, C.M.1    Baker, S.L.2    Jansen, K.3    Metzner, S.I.4    Sousa, M.C.5
  • 187
    • 84855303092 scopus 로고    scopus 로고
    • Chaperone receptors: Guiding proteins to intracellular compartments
    • [Electronic publication ahead of print]
    • V. Kriechbaumer, O. von Löffelholz, and B.M. Abell Chaperone receptors: guiding proteins to intracellular compartments Protoplasma 2011 [Electronic publication ahead of print]
    • (2011) Protoplasma
    • Kriechbaumer, V.1    Von Löffelholz, O.2    Abell, B.M.3
  • 188
    • 79851468985 scopus 로고    scopus 로고
    • Structural characterization of Escherichia coli BamE, a lipoprotein component of the β-barrel assembly machinery complex
    • K.H. Kim, H.-S. Kang, M. Okon, E. Escobar-Cabrera, L.P. McIntosh, and M. Paetzel Structural characterization of Escherichia coli BamE, a lipoprotein component of the β-barrel assembly machinery complex Biochemistry 50 2011 1081 1090
    • (2011) Biochemistry , vol.50 , pp. 1081-1090
    • Kim, K.H.1    Kang, H.-S.2    Okon, M.3    Escobar-Cabrera, E.4    McIntosh, L.P.5    Paetzel, M.6
  • 190
    • 0042565977 scopus 로고    scopus 로고
    • Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane. A study with pyrene-labelled phospholipids
    • S. Vanounou, A.H. Parola, and I. Fishov Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane. A study with pyrene-labelled phospholipids Mol. Microbiol. 49 2003 1067 1079
    • (2003) Mol. Microbiol. , vol.49 , pp. 1067-1079
    • Vanounou, S.1    Parola, A.H.2    Fishov, I.3
  • 191
    • 70350520053 scopus 로고    scopus 로고
    • The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential
    • G.J. Patel, S. Behrens-Kneip, O. Holst, and J.H. Kleinschmidt The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential Biochemistry 48 2009 10235 10245
    • (2009) Biochemistry , vol.48 , pp. 10235-10245
    • Patel, G.J.1    Behrens-Kneip, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 192
    • 0030756034 scopus 로고    scopus 로고
    • Folding of a bacterial outer membrane protein during passage through the periplasm
    • E.F. Eppens, N. Nouwen, and J. Tommassen Folding of a bacterial outer membrane protein during passage through the periplasm EMBO J. 16 1997 4295 4301
    • (1997) EMBO J. , vol.16 , pp. 4295-4301
    • Eppens, E.F.1    Nouwen, N.2    Tommassen, J.3
  • 193
    • 0026560272 scopus 로고
    • Dynamics of the exposure of epitopes on OmpF, an outer membrane protein of Escherichia coli
    • D. Fourel, S. Mizushima, and J.M. Pagès Dynamics of the exposure of epitopes on OmpF, an outer membrane protein of Escherichia coli Eur. J. Biochem. 206 1992 109 114
    • (1992) Eur. J. Biochem. , vol.206 , pp. 109-114
    • Fourel, D.1    Mizushima, S.2    Pagès, J.M.3
  • 194
    • 0024278694 scopus 로고
    • Targeting of porin to the outer membrane of Escherichia coli. Rate of trimer assembly and identification of a dimer intermediate
    • J. Reid, H. Fung, K. Gehring, P.E. Klebba, and H. Nikaido Targeting of porin to the outer membrane of Escherichia coli. Rate of trimer assembly and identification of a dimer intermediate J. Biol. Chem. 263 1988 7753 7759
    • (1988) J. Biol. Chem. , vol.263 , pp. 7753-7759
    • Reid, J.1    Fung, H.2    Gehring, K.3    Klebba, P.E.4    Nikaido, H.5
  • 195
    • 0021605388 scopus 로고
    • Assembly pathway of newly synthesized LamB protein an outer membrane protein of Escherichia coli K-12
    • G.H. Vos-Scheperkeuter, and B. Witholt Assembly pathway of newly synthesized LamB protein an outer membrane protein of Escherichia coli K-12 J. Mol. Biol. 175 1984 511 528
    • (1984) J. Mol. Biol. , vol.175 , pp. 511-528
    • Vos-Scheperkeuter, G.H.1    Witholt, B.2
  • 196
    • 77955463665 scopus 로고    scopus 로고
    • Nonconsecutive disulfide bond formation in an essential integral outer membrane protein
    • N. Ruiz, S.-S. Chng, A. Hiniker, D. Kahne, and T.J. Silhavy Nonconsecutive disulfide bond formation in an essential integral outer membrane protein Proc. Natl. Acad. Sci. U.S.A. 107 2010 12245 12250
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 12245-12250
    • Ruiz, N.1    Chng, S.-S.2    Hiniker, A.3    Kahne, D.4    Silhavy, T.J.5
  • 197
    • 79952300098 scopus 로고    scopus 로고
    • Lipoprotein LptE is required for the assembly of LptD by the beta-barrel assembly machine in the outer membrane of Escherichia coli
    • G. Chimalakonda, N. Ruiz, S.-S. Chng, R.A. Garner, D. Kahne, and T.J. Silhavy Lipoprotein LptE is required for the assembly of LptD by the beta-barrel assembly machine in the outer membrane of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 108 2011 2492 2497
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 2492-2497
    • Chimalakonda, G.1    Ruiz, N.2    Chng, S.-S.3    Garner, R.A.4    Kahne, D.5    Silhavy, T.J.6
  • 198
    • 79961225871 scopus 로고    scopus 로고
    • PNAS Plus: Sequential and spatially restricted interactions of assembly factors with an autotransporter {beta} domain
    • R. Ieva, P. Tian, J.H. Peterson, and H.D. Bernstein PNAS Plus: sequential and spatially restricted interactions of assembly factors with an autotransporter {beta} domain Proc. Natl. Acad. Sci. U.S.A. 108 31 2011 E383 E391
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , Issue.31
    • Ieva, R.1    Tian, P.2    Peterson, J.H.3    Bernstein, H.D.4
  • 200
    • 0026770209 scopus 로고
    • Refolding and oriented insertion of a membrane protein into a lipid bilayer
    • T. Surrey, and F. Jähnig Refolding and oriented insertion of a membrane protein into a lipid bilayer Proc. Natl. Acad. Sci. U.S.A. 89 1992 7457 7461
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7457-7461
    • Surrey, T.1    Jähnig, F.2
  • 201
    • 0025215603 scopus 로고
    • Reconstitution of protein translocation from detergent-solubilized Escherichia coli inverted vesicles: PrlA protein-deficient vesicles efficiently translocate precursor proteins
    • M. Watanabe, C.V. Nicchitta, and G. Blobel Reconstitution of protein translocation from detergent-solubilized Escherichia coli inverted vesicles: PrlA protein-deficient vesicles efficiently translocate precursor proteins Proc. Natl. Acad. Sci. U.S.A. 87 1990 1960 1964
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 1960-1964
    • Watanabe, M.1    Nicchitta, C.V.2    Blobel, G.3
  • 202
    • 0025214263 scopus 로고
    • Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli
    • A.L. Davidson, and H. Nikaido Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli J. Biol. Chem. 265 1990 4254 4260
    • (1990) J. Biol. Chem. , vol.265 , pp. 4254-4260
    • Davidson, A.L.1    Nikaido, H.2
  • 203
    • 34249797024 scopus 로고    scopus 로고
    • Complete reconstitution of an ATP-binding cassette transporter LolCDE complex from separately isolated subunits
    • K. Kanamaru, N. Taniguchi, S. Miyamoto, S.-i. Narita, and H. Tokuda Complete reconstitution of an ATP-binding cassette transporter LolCDE complex from separately isolated subunits FEBS J. 274 2007 3034 3043
    • (2007) FEBS J. , vol.274 , pp. 3034-3043
    • Kanamaru, K.1    Taniguchi, N.2    Miyamoto, S.3    Narita, S.-I.4    Tokuda, H.5


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