메뉴 건너뛰기




Volumn 1843, Issue 8, 2014, Pages 1509-1516

Secretion of Bacterial Lipoproteins: Through the Cytoplasmic Membrane, the Periplasm and Beyond

Author keywords

Bacterial envelope; Chaperone; Lipoprotein; Membrane protein; Postranslational modification; Protein secretion

Indexed keywords

ABC TRANSPORTER; ACYLTRANSFERASE; BACTERIUM LIPOPROTEIN; CHAPERONE; DIACYLGLYCEROL; LIPOPROTEIN; LIPOPROTEIN RECEPTOR; MALTOSE BINDING PROTEIN; SIGNAL PEPTIDASE II; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

EID: 84902276774     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.04.022     Document Type: Review
Times cited : (164)

References (136)
  • 1
    • 0014594651 scopus 로고
    • Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure
    • Braun V., Rehn K. Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure. Eur. J. Biochem. 1969, 10:426-438.
    • (1969) Eur. J. Biochem. , vol.10 , pp. 426-438
    • Braun, V.1    Rehn, K.2
  • 2
    • 0015611501 scopus 로고
    • Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murein-lipoprotein of the Escherichia coli outer membrane
    • Hantke K., Braun V. Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murein-lipoprotein of the Escherichia coli outer membrane. Eur. J. Biochem. 1973, 34:284-296.
    • (1973) Eur. J. Biochem. , vol.34 , pp. 284-296
    • Hantke, K.1    Braun, V.2
  • 3
    • 0024393453 scopus 로고
    • The structure of signal peptides from bacterial lipoproteins
    • von Heijne G. The structure of signal peptides from bacterial lipoproteins. Protein Eng. 1989, 2:531-534.
    • (1989) Protein Eng. , vol.2 , pp. 531-534
    • von Heijne, G.1
  • 4
    • 0003094448 scopus 로고
    • Bacterial lipoproteins
    • CRC Press, Boca Raton, M.J. Schlesinger (Ed.)
    • Sankaran K., Wu H.C. Bacterial lipoproteins. Lipid modifications of proteins 1993, 163-181. CRC Press, Boca Raton. M.J. Schlesinger (Ed.).
    • (1993) Lipid modifications of proteins , pp. 163-181
    • Sankaran, K.1    Wu, H.C.2
  • 5
    • 33645972887 scopus 로고    scopus 로고
    • A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins
    • Babu M.M., Priya M.L., Selvan A.T., Madera M., Gough J., Aravind L., Sankaran K. A database of bacterial lipoproteins (DOLOP) with functional assignments to predicted lipoproteins. J. Bacteriol. 2006, 188:2761-2773.
    • (2006) J. Bacteriol. , vol.188 , pp. 2761-2773
    • Babu, M.M.1    Priya, M.L.2    Selvan, A.T.3    Madera, M.4    Gough, J.5    Aravind, L.6    Sankaran, K.7
  • 6
    • 30744477217 scopus 로고    scopus 로고
    • Lipoprotein computational prediction in spirochaetal genomes
    • Setubal J.C., Reis M., Matsunaga J., Haake D.A. Lipoprotein computational prediction in spirochaetal genomes. Microbiology 2006, 152:113-121.
    • (2006) Microbiology , vol.152 , pp. 113-121
    • Setubal, J.C.1    Reis, M.2    Matsunaga, J.3    Haake, D.A.4
  • 7
    • 77952816250 scopus 로고    scopus 로고
    • Translocation of Borrelia burgdorferi surface lipoprotein OspA through the outer membrane requires an unfolded conformation and can initiate at the C-terminus
    • Schulze R.J., Chen S., Kumru O.S., Zückert W.R. Translocation of Borrelia burgdorferi surface lipoprotein OspA through the outer membrane requires an unfolded conformation and can initiate at the C-terminus. Mol. Microbiol. 2010, 76:1266-1278.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1266-1278
    • Schulze, R.J.1    Chen, S.2    Kumru, O.S.3    Zückert, W.R.4
  • 8
    • 0034674154 scopus 로고    scopus 로고
    • Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution
    • Shu W., Liu J., Ji H., Lu M. Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution. J. Mol. Biol. 2000, 299:1101-1112.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1101-1112
    • Shu, W.1    Liu, J.2    Ji, H.3    Lu, M.4
  • 9
    • 84888322111 scopus 로고    scopus 로고
    • Crystal structure of the infectious phenotype-associated outer surface protein BBA66 from the Lyme disease agent Borrelia burgdorferi
    • Brangulis K., Petrovskis I., Kazaks A., Tars K., Ranka R. Crystal structure of the infectious phenotype-associated outer surface protein BBA66 from the Lyme disease agent Borrelia burgdorferi. Ticks Tick Borne Dis. 2014, 5:63-68.
    • (2014) Ticks Tick Borne Dis. , vol.5 , pp. 63-68
    • Brangulis, K.1    Petrovskis, I.2    Kazaks, A.3    Tars, K.4    Ranka, R.5
  • 10
    • 84880131857 scopus 로고    scopus 로고
    • A call to order at the spirochaetal host-pathogen interface
    • Zückert W.R. A call to order at the spirochaetal host-pathogen interface. Mol. Microbiol. 2013, 89:207-211.
    • (2013) Mol. Microbiol. , vol.89 , pp. 207-211
    • Zückert, W.R.1
  • 11
    • 3843095033 scopus 로고    scopus 로고
    • Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway
    • Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W. Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway. J. Biol. Chem. 2004, 279:31026-31032.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31026-31032
    • Froderberg, L.1    Houben, E.N.2    Baars, L.3    Luirink, J.4    de Gier, J.W.5
  • 13
    • 27844443566 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea
    • Dilks K., Gimenez M.I., Pohlschröder M. Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea. J. Bacteriol. 2005, 187:8104-8113.
    • (2005) J. Bacteriol. , vol.187 , pp. 8104-8113
    • Dilks, K.1    Gimenez, M.I.2    Pohlschröder, M.3
  • 14
    • 36549088956 scopus 로고    scopus 로고
    • Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins
    • Gimenez M.I., Dilks K., Pohlschröder M. Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins. Mol. Microbiol. 2007, 66:1597-1606.
    • (2007) Mol. Microbiol. , vol.66 , pp. 1597-1606
    • Gimenez, M.I.1    Dilks, K.2    Pohlschröder, M.3
  • 17
    • 84873549702 scopus 로고    scopus 로고
    • Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain
    • Feltcher M.E., Gibbons H.S., Ligon L.S., Braunstein M. Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain. J. Bacteriol. 2013, 195:672-681.
    • (2013) J. Bacteriol. , vol.195 , pp. 672-681
    • Feltcher, M.E.1    Gibbons, H.S.2    Ligon, L.S.3    Braunstein, M.4
  • 18
    • 58149295961 scopus 로고    scopus 로고
    • Lipoprotein biogenesis in gram-positive bacteria: knowing when to hold 'em, knowing when to fold 'em
    • Hutchings M.I., Palmer T., Harrington D.J., Sutcliffe I.C. Lipoprotein biogenesis in gram-positive bacteria: knowing when to hold 'em, knowing when to fold 'em. Trends Microbiol. 2009, 17:13-21.
    • (2009) Trends Microbiol. , vol.17 , pp. 13-21
    • Hutchings, M.I.1    Palmer, T.2    Harrington, D.J.3    Sutcliffe, I.C.4
  • 19
    • 0028067877 scopus 로고
    • Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol
    • Sankaran K., Wu H.C. Lipid modification of bacterial prolipoprotein. Transfer of diacylglyceryl moiety from phosphatidylglycerol. J. Biol. Chem. 1994, 269:19701-19706.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19701-19706
    • Sankaran, K.1    Wu, H.C.2
  • 20
    • 19744376674 scopus 로고    scopus 로고
    • Global topology analysis of the Escherichia coli inner membrane proteome
    • Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Global topology analysis of the Escherichia coli inner membrane proteome. Science 2005, 308:1321-1323.
    • (2005) Science , vol.308 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5    von Heijne, G.6
  • 21
    • 0028817888 scopus 로고
    • Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions
    • Qi H.Y., Sankaran K., Gan K., Wu H.C. Structure-function relationship of bacterial prolipoprotein diacylglyceryl transferase: functionally significant conserved regions. J. Bacteriol. 1995, 177:6820-6824.
    • (1995) J. Bacteriol. , vol.177 , pp. 6820-6824
    • Qi, H.Y.1    Sankaran, K.2    Gan, K.3    Wu, H.C.4
  • 22
    • 0031002075 scopus 로고    scopus 로고
    • Roles of histidine-103 and tyrosine-235 in the function of the prolipoprotein diacylglyceryl transferase of Escherichia coli
    • Sankaran K., Gan K., Rash B., Qi H.Y., Wu H.C., Rick P.D. Roles of histidine-103 and tyrosine-235 in the function of the prolipoprotein diacylglyceryl transferase of Escherichia coli. J. Bacteriol. 1997, 179:2944-2948.
    • (1997) J. Bacteriol. , vol.179 , pp. 2944-2948
    • Sankaran, K.1    Gan, K.2    Rash, B.3    Qi, H.Y.4    Wu, H.C.5    Rick, P.D.6
  • 23
    • 55349122529 scopus 로고    scopus 로고
    • Localization and characterization of prolipoprotein diacylglyceryl transferase (Lgt) critical in bacterial lipoprotein biosynthesis
    • Selvan A.T., Sankaran K. Localization and characterization of prolipoprotein diacylglyceryl transferase (Lgt) critical in bacterial lipoprotein biosynthesis. Biochimie 2008, 90:1647-1655.
    • (2008) Biochimie , vol.90 , pp. 1647-1655
    • Selvan, A.T.1    Sankaran, K.2
  • 24
    • 0012295404 scopus 로고
    • Post-translational modification and processing of Escherichia coli prolipoprotein in vitro
    • Tokunaga M., Tokunaga H., Wu H.C. Post-translational modification and processing of Escherichia coli prolipoprotein in vitro. Proc. Natl. Acad. Sci. U. S. A. 1982, 79:2255-2259.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 2255-2259
    • Tokunaga, M.1    Tokunaga, H.2    Wu, H.C.3
  • 25
    • 0026063242 scopus 로고
    • Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II)
    • Munoa F.J., Miller K.W., Beers R., Graham M., Wu H.C. Membrane topology of Escherichia coli prolipoprotein signal peptidase (signal peptidase II). J. Biol. Chem. 1991, 266:17667-17672.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17667-17672
    • Munoa, F.J.1    Miller, K.W.2    Beers, R.3    Graham, M.4    Wu, H.C.5
  • 26
    • 0033214086 scopus 로고    scopus 로고
    • The potential active site of the lipoprotein-specific (type II) signal peptidase of Bacillus subtilis
    • Tjalsma H., Zanen G., Venema G., Bron S., van Dijl J.M. The potential active site of the lipoprotein-specific (type II) signal peptidase of Bacillus subtilis. J. Biol. Chem. 1999, 274:28191-28197.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28191-28197
    • Tjalsma, H.1    Zanen, G.2    Venema, G.3    Bron, S.4    van Dijl, J.M.5
  • 27
    • 0021800753 scopus 로고
    • Inhibition of prolipoprotein signal peptidase by globomycin
    • Dev I.K., Harvey R.J., Ray P.H. Inhibition of prolipoprotein signal peptidase by globomycin. J. Biol. Chem. 1985, 260:5891-5894.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5891-5894
    • Dev, I.K.1    Harvey, R.J.2    Ray, P.H.3
  • 28
    • 34250303119 scopus 로고    scopus 로고
    • Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family
    • Vidal-Ingigliardi D., Lewenza S., Buddelmeijer N. Identification of essential residues in apolipoprotein N-acyl transferase, a member of the CN hydrolase family. J. Bacteriol. 2007, 189:4456-4464.
    • (2007) J. Bacteriol. , vol.189 , pp. 4456-4464
    • Vidal-Ingigliardi, D.1    Lewenza, S.2    Buddelmeijer, N.3
  • 30
    • 0023032318 scopus 로고
    • Transfer of fatty acids from the 1-position of phosphatidylethanolamine to the major outer membrane lipoprotein of Escherichia coli
    • Jackowski S., Rock C.O. Transfer of fatty acids from the 1-position of phosphatidylethanolamine to the major outer membrane lipoprotein of Escherichia coli. J. Biol. Chem. 1986, 261:11328-11333.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11328-11333
    • Jackowski, S.1    Rock, C.O.2
  • 31
    • 0025871351 scopus 로고
    • Phosphatidylethanolamine is not essential for the N-acylation of apolipoprotein in Escherichia coli
    • Gupta S.D., Dowhan W., Wu H.C. Phosphatidylethanolamine is not essential for the N-acylation of apolipoprotein in Escherichia coli. J. Biol. Chem. 1991, 266:9983-9986.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9983-9986
    • Gupta, S.D.1    Dowhan, W.2    Wu, H.C.3
  • 32
    • 80051503015 scopus 로고    scopus 로고
    • Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase
    • Hillmann F., Argentini M., Buddelmeijer N. Kinetics and phospholipid specificity of apolipoprotein N-acyltransferase. J. Biol. Chem. 2011, 286:27936-27946.
    • (2011) J. Biol. Chem. , vol.286 , pp. 27936-27946
    • Hillmann, F.1    Argentini, M.2    Buddelmeijer, N.3
  • 33
    • 84870061381 scopus 로고    scopus 로고
    • Lipoproteins in bacteria: structures and biosynthetic pathways
    • Nakayama H., Kurokawa K., Lee B.L. Lipoproteins in bacteria: structures and biosynthetic pathways. FEBS J. 2012, 279:4247-4268.
    • (2012) FEBS J. , vol.279 , pp. 4247-4268
    • Nakayama, H.1    Kurokawa, K.2    Lee, B.L.3
  • 34
    • 12544257510 scopus 로고    scopus 로고
    • Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli
    • Robichon C., Vidal-Ingigliardi D., Pugsley A.P. Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli. J. Biol. Chem. 2005, 280:974-983.
    • (2005) J. Biol. Chem. , vol.280 , pp. 974-983
    • Robichon, C.1    Vidal-Ingigliardi, D.2    Pugsley, A.P.3
  • 35
    • 0032871073 scopus 로고    scopus 로고
    • Identification and characterization of a determinant (eep) on the Enterococcus faecalis chromosome that is involved in production of the peptide sex pheromone cAD1
    • An F.Y., Sulavik M.C., Clewell D.B. Identification and characterization of a determinant (eep) on the Enterococcus faecalis chromosome that is involved in production of the peptide sex pheromone cAD1. J. Bacteriol. 1999, 181:5915-5921.
    • (1999) J. Bacteriol. , vol.181 , pp. 5915-5921
    • An, F.Y.1    Sulavik, M.C.2    Clewell, D.B.3
  • 36
    • 0036157479 scopus 로고    scopus 로고
    • CcfA, the genetic determinant for the cCF10 peptide pheromone in Enterococcus faecalis OG1RF
    • Antiporta M.H., Dunny G.M. ccfA, the genetic determinant for the cCF10 peptide pheromone in Enterococcus faecalis OG1RF. J. Bacteriol. 2002, 184:1155-1162.
    • (2002) J. Bacteriol. , vol.184 , pp. 1155-1162
    • Antiporta, M.H.1    Dunny, G.M.2
  • 37
    • 38949108711 scopus 로고    scopus 로고
    • Characterization of the sequence specificity determinants required for processing and control of sex pheromone by the intramembrane protease Eep and the plasmid-encoded protein PrgY
    • Chandler J.R., Dunny G.M. Characterization of the sequence specificity determinants required for processing and control of sex pheromone by the intramembrane protease Eep and the plasmid-encoded protein PrgY. J. Bacteriol. 2008, 190:1172-1183.
    • (2008) J. Bacteriol. , vol.190 , pp. 1172-1183
    • Chandler, J.R.1    Dunny, G.M.2
  • 38
    • 46049119823 scopus 로고    scopus 로고
    • Lipoprotein signal peptides are processed by Lsp and Eep of Streptococcus uberis
    • Denham E.L., Ward P.N., Leigh J.A. Lipoprotein signal peptides are processed by Lsp and Eep of Streptococcus uberis. J. Bacteriol. 2008, 190:4641-4647.
    • (2008) J. Bacteriol. , vol.190 , pp. 4641-4647
    • Denham, E.L.1    Ward, P.N.2    Leigh, J.A.3
  • 39
    • 84877824977 scopus 로고    scopus 로고
    • The TIKI/TraB/PrgY family: a common protease fold for cell signaling from bacteria to metazoa?
    • Bazan J.F., Macdonald B.T., He X. The TIKI/TraB/PrgY family: a common protease fold for cell signaling from bacteria to metazoa?. Dev. Cell 2013, 25:225-227.
    • (2013) Dev. Cell , vol.25 , pp. 225-227
    • Bazan, J.F.1    Macdonald, B.T.2    He, X.3
  • 40
    • 21844463033 scopus 로고    scopus 로고
    • Specific control of endogenous cCF10 pheromone by a conserved domain of the pCF10-encoded regulatory protein PrgY in Enterococcus faecalis
    • Chandler J.R., Flynn A.R., Bryan E.M., Dunny G.M. Specific control of endogenous cCF10 pheromone by a conserved domain of the pCF10-encoded regulatory protein PrgY in Enterococcus faecalis. J. Bacteriol. 2005, 187:4830-4843.
    • (2005) J. Bacteriol. , vol.187 , pp. 4830-4843
    • Chandler, J.R.1    Flynn, A.R.2    Bryan, E.M.3    Dunny, G.M.4
  • 41
    • 0021759116 scopus 로고
    • Nine amino acid residues at the NH2-terminal of lipoprotein are sufficient for its modification, processing, and localization in the outer membrane of Escherichia coli
    • Ghrayeb J., Inouye M. Nine amino acid residues at the NH2-terminal of lipoprotein are sufficient for its modification, processing, and localization in the outer membrane of Escherichia coli. J. Biol. Chem. 1984, 259:463-467.
    • (1984) J. Biol. Chem. , vol.259 , pp. 463-467
    • Ghrayeb, J.1    Inouye, M.2
  • 42
    • 0024279918 scopus 로고
    • A single amino acid determinant of the membrane localization of lipoproteins in E. coli
    • Yamaguchi K., Yu F., Inouye M. A single amino acid determinant of the membrane localization of lipoproteins in E. coli. Cell 1988, 53:423-432.
    • (1988) Cell , vol.53 , pp. 423-432
    • Yamaguchi, K.1    Yu, F.2    Inouye, M.3
  • 43
    • 0026010463 scopus 로고
    • The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity
    • Gennity J.M., Inouye M. The protein sequence responsible for lipoprotein membrane localization in Escherichia coli exhibits remarkable specificity. J. Biol. Chem. 1991, 266:16458-16464.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16458-16464
    • Gennity, J.M.1    Inouye, M.2
  • 44
    • 0032701349 scopus 로고    scopus 로고
    • Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection
    • Seydel A., Gounon P., Pugsley A.P. Testing the '+2 rule' for lipoprotein sorting in the Escherichia coli cell envelope with a new genetic selection. Mol. Microbiol. 1999, 34:810-821.
    • (1999) Mol. Microbiol. , vol.34 , pp. 810-821
    • Seydel, A.1    Gounon, P.2    Pugsley, A.P.3
  • 45
    • 33646575276 scopus 로고    scopus 로고
    • Direct visualization of red fluorescent lipoproteins indicates conservation of the membrane sorting rules in the family Enterobacteriaceae
    • Lewenza S., Vidal-Ingigliardi D., Pugsley A.P. Direct visualization of red fluorescent lipoproteins indicates conservation of the membrane sorting rules in the family Enterobacteriaceae. J. Bacteriol. 2006, 188:3516-3524.
    • (2006) J. Bacteriol. , vol.188 , pp. 3516-3524
    • Lewenza, S.1    Vidal-Ingigliardi, D.2    Pugsley, A.P.3
  • 46
    • 51549111175 scopus 로고    scopus 로고
    • Novel inner membrane retention signals in Pseudomonas aeruginosa lipoproteins
    • Lewenza S., Mhlanga M.M., Pugsley A.P. Novel inner membrane retention signals in Pseudomonas aeruginosa lipoproteins. J. Bacteriol. 2008, 190:6119-6125.
    • (2008) J. Bacteriol. , vol.190 , pp. 6119-6125
    • Lewenza, S.1    Mhlanga, M.M.2    Pugsley, A.P.3
  • 47
    • 0014346151 scopus 로고
    • Areas of adhesion between wall and membrane of Escherichia coli
    • Bayer M.E. Areas of adhesion between wall and membrane of Escherichia coli. J. Gen. Microbiol. 1968, 53:395-404.
    • (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
    • Bayer M.E. Zones of membrane adhesion in the cryofixed envelope of Escherichia coli. J. Struct. Biol. 1991, 107:268-280.
    • (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
    • Kellenberger E. The 'Bayer bridges' confronted with results from improved electron microscopy methods. Mol. Microbiol. 1990, 4:697-705.
    • (1990) Mol. Microbiol. , vol.4 , pp. 697-705
    • Kellenberger, E.1
  • 50
    • 0028981022 scopus 로고
    • A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane
    • Matsuyama S., Tajima T., Tokuda H. A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane. EMBO J. 1995, 14:3365-3372.
    • (1995) EMBO J. , vol.14 , pp. 3365-3372
    • Matsuyama, S.1    Tajima, T.2    Tokuda, H.3
  • 51
    • 0032515174 scopus 로고    scopus 로고
    • Genetic analyses of the in vivo function of LolA, a periplasmic chaperone involved in the outer membrane localization of Escherichia coli lipoproteins
    • Tajima T., Yokota N., Matsuyama S., Tokuda H. Genetic analyses of the in vivo function of LolA, a periplasmic chaperone involved in the outer membrane localization of Escherichia coli lipoproteins. FEBS Lett. 1998, 439:51-54.
    • (1998) FEBS Lett. , vol.439 , pp. 51-54
    • Tajima, T.1    Yokota, N.2    Matsuyama, S.3    Tokuda, H.4
  • 52
    • 0030663775 scopus 로고    scopus 로고
    • A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli
    • Matsuyama S., Yokota N., Tokuda H. A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli. EMBO J. 1997, 16:6947-6955.
    • (1997) EMBO J. , vol.16 , pp. 6947-6955
    • Matsuyama, S.1    Yokota, N.2    Tokuda, H.3
  • 53
    • 0034750231 scopus 로고    scopus 로고
    • Deletion of lolB, encoding an outer membrane lipoprotein, is lethal for Escherichia coli and causes accumulation of lipoprotein localization intermediates in the periplasm
    • Tanaka K., Matsuyama S.I., Tokuda H. Deletion of lolB, encoding an outer membrane lipoprotein, is lethal for Escherichia coli and causes accumulation of lipoprotein localization intermediates in the periplasm. J. Bacteriol. 2001, 183:6538-6542.
    • (2001) J. Bacteriol. , vol.183 , pp. 6538-6542
    • Tanaka, K.1    Matsuyama, S.I.2    Tokuda, H.3
  • 54
    • 0038602740 scopus 로고    scopus 로고
    • Crystal structures of bacterial lipoprotein localization factors, LolA and LolB
    • Takeda K., Miyatake H., Yokota N., Matsuyama S., Tokuda H., Miki K. Crystal structures of bacterial lipoprotein localization factors, LolA and LolB. EMBO J. 2003, 22:3199-3209.
    • (2003) EMBO J. , vol.22 , pp. 3199-3209
    • Takeda, K.1    Miyatake, H.2    Yokota, N.3    Matsuyama, S.4    Tokuda, H.5    Miki, K.6
  • 55
    • 44749084464 scopus 로고    scopus 로고
    • A short helix in the C-terminal region of LolA is important for the specific membrane localization of lipoproteins
    • Okuda S., Watanabe S., Tokuda H. A short helix in the C-terminal region of LolA is important for the specific membrane localization of lipoproteins. FEBS Lett. 2008, 582:2247-2251.
    • (2008) FEBS Lett. , vol.582 , pp. 2247-2251
    • Okuda, S.1    Watanabe, S.2    Tokuda, H.3
  • 56
    • 54449086634 scopus 로고    scopus 로고
    • Opening and closing of the hydrophobic cavity of LolA coupled to lipoprotein binding and release
    • Oguchi Y., Takeda K., Watanabe S., Yokota N., Miki K., Tokuda H. Opening and closing of the hydrophobic cavity of LolA coupled to lipoprotein binding and release. J. Biol. Chem. 2008, 283:25414-25420.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25414-25420
    • Oguchi, Y.1    Takeda, K.2    Watanabe, S.3    Yokota, N.4    Miki, K.5    Tokuda, H.6
  • 57
    • 0035850777 scopus 로고    scopus 로고
    • Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB
    • Miyamoto A., Matsuyama S., Tokuda H. Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB. Biochem. Biophys. Res. Commun. 2001, 287:1125-1128.
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 1125-1128
    • Miyamoto, A.1    Matsuyama, S.2    Tokuda, H.3
  • 58
    • 27144449975 scopus 로고    scopus 로고
    • Mechanisms underlying energy-independent transfer of lipoproteins from LolA to LolB, which have similar unclosed β-barrel structures
    • Taniguchi N., Matsuyama S., Tokuda H. Mechanisms underlying energy-independent transfer of lipoproteins from LolA to LolB, which have similar unclosed β-barrel structures. J. Biol. Chem. 2005, 280:34481-34488.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34481-34488
    • Taniguchi, N.1    Matsuyama, S.2    Tokuda, H.3
  • 59
    • 78049387443 scopus 로고    scopus 로고
    • A periplasmic LolA derivative with a lethal disulfide bond activates the Cpx stress response system
    • Tao K., Watanabe S., Narita S., Tokuda H. A periplasmic LolA derivative with a lethal disulfide bond activates the Cpx stress response system. J. Bacteriol. 2010, 192:5657-5662.
    • (2010) J. Bacteriol. , vol.192 , pp. 5657-5662
    • Tao, K.1    Watanabe, S.2    Narita, S.3    Tokuda, H.4
  • 60
    • 54449093948 scopus 로고    scopus 로고
    • Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA
    • Watanabe S., Oguchi Y., Takeda K., Miki K., Tokuda H. Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA. J. Biol. Chem. 2008, 283:25421-25427.
    • (2008) J. Biol. Chem. , vol.283 , pp. 25421-25427
    • Watanabe, S.1    Oguchi, Y.2    Takeda, K.3    Miki, K.4    Tokuda, H.5
  • 61
    • 84898670675 scopus 로고    scopus 로고
    • Roles of the protruding loop of factor B essential for the localization of lipoproteins (LolB) in the anchoring of bacterial triacylated proteins to the outer membrane
    • Hayashi Y., Tsurumizu R., Tsukahara J., Takeda K., Narita S.I., Mori M., Miki K., Tokuda H. Roles of the protruding loop of factor B essential for the localization of lipoproteins (LolB) in the anchoring of bacterial triacylated proteins to the outer membrane. J. Biol. Chem. 2014, 289:10530-10539.
    • (2014) J. Biol. Chem. , vol.289 , pp. 10530-10539
    • Hayashi, Y.1    Tsurumizu, R.2    Tsukahara, J.3    Takeda, K.4    Narita, S.I.5    Mori, M.6    Miki, K.7    Tokuda, H.8
  • 62
    • 80053280679 scopus 로고    scopus 로고
    • Lipoprotein sorting in bacteria
    • Okuda S., Tokuda H. Lipoprotein sorting in bacteria. Annu. Rev. Microbiol. 2011, 65:239-259.
    • (2011) Annu. Rev. Microbiol. , vol.65 , pp. 239-259
    • Okuda, S.1    Tokuda, H.2
  • 65
    • 68749109764 scopus 로고    scopus 로고
    • Dissection of LolB function-lipoprotein binding, membrane targeting and incorporation of lipoproteins into lipid bilayers
    • Tsukahara J., Mukaiyama K., Okuda S., Narita S., Tokuda H. Dissection of LolB function-lipoprotein binding, membrane targeting and incorporation of lipoproteins into lipid bilayers. FEBS J. 2009, 276:4496-4504.
    • (2009) FEBS J. , vol.276 , pp. 4496-4504
    • Tsukahara, J.1    Mukaiyama, K.2    Okuda, S.3    Narita, S.4    Tokuda, H.5
  • 66
    • 33646003856 scopus 로고    scopus 로고
    • Genetic analysis of the mode of interplay between an ATPase subunit and membrane subunits of the lipoprotein-releasing ATP-binding cassette transporter LolCDE
    • Ito Y., Matsuzawa H., Matsuyama S., Narita S., Tokuda H. Genetic analysis of the mode of interplay between an ATPase subunit and membrane subunits of the lipoprotein-releasing ATP-binding cassette transporter LolCDE. J. Bacteriol. 2006, 188:2856-2864.
    • (2006) J. Bacteriol. , vol.188 , pp. 2856-2864
    • Ito, Y.1    Matsuzawa, H.2    Matsuyama, S.3    Narita, S.4    Tokuda, H.5
  • 67
    • 0032484007 scopus 로고    scopus 로고
    • LolA-dependent release of a lipid-modified protein from the inner membrane of Escherichia coli requires nucleoside triphosphate
    • Yakushi T., Yokota N., Matsuyama S., Tokuda H. LolA-dependent release of a lipid-modified protein from the inner membrane of Escherichia coli requires nucleoside triphosphate. J. Biol. Chem. 1998, 273:32576-32581.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32576-32581
    • Yakushi, T.1    Yokota, N.2    Matsuyama, S.3    Tokuda, H.4
  • 68
    • 0033787084 scopus 로고    scopus 로고
    • A new ABC transporter mediating the detachment of lipid-modified proteins from membranes
    • Yakushi T., Masuda K., Narita S., Matsuyama S., Tokuda H. A new ABC transporter mediating the detachment of lipid-modified proteins from membranes. Nat. Cell Biol. 2000, 2:212-218.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 212-218
    • Yakushi, T.1    Masuda, K.2    Narita, S.3    Matsuyama, S.4    Tokuda, H.5
  • 70
    • 0037044719 scopus 로고    scopus 로고
    • Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals
    • Fukuda A., Matsuyama S., Hara T., Nakayama J., Nagasawa H., Tokuda H. Aminoacylation of the N-terminal cysteine is essential for Lol-dependent release of lipoproteins from membranes but does not depend on lipoprotein sorting signals. J. Biol. Chem. 2002, 277:43512-43518.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43512-43518
    • Fukuda, A.1    Matsuyama, S.2    Hara, T.3    Nakayama, J.4    Nagasawa, H.5    Tokuda, H.6
  • 71
    • 0027185234 scopus 로고
    • Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase
    • Gupta S.D., Gan K., Schmid M.B., Wu H.C. Characterization of a temperature-sensitive mutant of Salmonella typhimurium defective in apolipoprotein N-acyltransferase. J. Biol. Chem. 1993, 268:16551-16556.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16551-16556
    • Gupta, S.D.1    Gan, K.2    Schmid, M.B.3    Wu, H.C.4
  • 72
    • 80052551712 scopus 로고    scopus 로고
    • Overexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase
    • Narita S., Tokuda H. Overexpression of LolCDE allows deletion of the Escherichia coli gene encoding apolipoprotein N-acyltransferase. J. Bacteriol. 2011, 193:4832-4840.
    • (2011) J. Bacteriol. , vol.193 , pp. 4832-4840
    • Narita, S.1    Tokuda, H.2
  • 73
    • 84871722765 scopus 로고    scopus 로고
    • Functional differentiation of structurally similar membrane subunits of the ABC transporter LolCDE complex
    • Mizutani M., Mukaiyama K., Xiao J., Mori M., Satou R., Narita S., Okuda S., Tokuda H. Functional differentiation of structurally similar membrane subunits of the ABC transporter LolCDE complex. FEBS Lett. 2013, 587:23-29.
    • (2013) FEBS Lett. , vol.587 , pp. 23-29
    • Mizutani, M.1    Mukaiyama, K.2    Xiao, J.3    Mori, M.4    Satou, R.5    Narita, S.6    Okuda, S.7    Tokuda, H.8
  • 74
    • 65249085615 scopus 로고    scopus 로고
    • Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB
    • Okuda S., Tokuda H. 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. 2009, 106:5877-5882.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 5877-5882
    • Okuda, S.1    Tokuda, H.2
  • 75
    • 0037188471 scopus 로고    scopus 로고
    • Elucidation of the function of lipoprotein- sorting signals that determine membrane localization
    • Masuda K., Matsuyama S., Tokuda H. Elucidation of the function of lipoprotein- sorting signals that determine membrane localization. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:7390-7395.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7390-7395
    • Masuda, K.1    Matsuyama, S.2    Tokuda, H.3
  • 76
    • 0141890241 scopus 로고    scopus 로고
    • Mechanism underlying the inner membrane retention of Escherichia coli lipoproteins caused by Lol avoidance signals
    • Hara T., Matsuyama S., Tokuda H. Mechanism underlying the inner membrane retention of Escherichia coli lipoproteins caused by Lol avoidance signals. J. Biol. Chem. 2003, 278:40408-40414.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40408-40414
    • Hara, T.1    Matsuyama, S.2    Tokuda, H.3
  • 77
    • 0023441713 scopus 로고
    • Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase
    • d'Enfert C., Ryter A., Pugsley A.P. Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase. EMBO J. 1987, 6:3531-3538.
    • (1987) EMBO J. , vol.6 , pp. 3531-3538
    • d'Enfert, C.1    Ryter, A.2    Pugsley, A.P.3
  • 78
    • 0028308286 scopus 로고
    • Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization
    • Anderson J.E., Sparling P.F., Cornelissen C.N. Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization. J. Bacteriol. 1994, 176:3162-3170.
    • (1994) J. Bacteriol. , vol.176 , pp. 3162-3170
    • Anderson, J.E.1    Sparling, P.F.2    Cornelissen, C.N.3
  • 79
    • 84884219205 scopus 로고    scopus 로고
    • Conserved regions of gonococcal TbpB are critical for surface exposure and transferrin iron utilization
    • Ostberg K.L., DeRocco A.J., Mistry S.D., Dickinson M.K., Cornelissen C.N. Conserved regions of gonococcal TbpB are critical for surface exposure and transferrin iron utilization. Infect. Immun. 2013, 81:3442-3450.
    • (2013) Infect. Immun. , vol.81 , pp. 3442-3450
    • Ostberg, K.L.1    DeRocco, A.J.2    Mistry, S.D.3    Dickinson, M.K.4    Cornelissen, C.N.5
  • 80
    • 0031984119 scopus 로고    scopus 로고
    • Molecular characterization of LbpB, the second lactoferrin-binding protein of Neisseria meningitidis
    • Pettersson A., Prinz T., Umar A., van der Biezen J., Tommassen J. Molecular characterization of LbpB, the second lactoferrin-binding protein of Neisseria meningitidis. Mol. Microbiol. 1998, 27:599-610.
    • (1998) Mol. Microbiol. , vol.27 , pp. 599-610
    • Pettersson, A.1    Prinz, T.2    Umar, A.3    van der Biezen, J.4    Tommassen, J.5
  • 81
    • 27444447753 scopus 로고    scopus 로고
    • Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages
    • Leuzzi R., Serino L., Scarselli M., Savino S., Fontana M.R., Monaci E., Taddei A., Fischer G., Rappuoli R., Pizza M. Ng-MIP, a surface-exposed lipoprotein of Neisseria gonorrhoeae, has a peptidyl-prolyl cis/trans isomerase (PPIase) activity and is involved in persistence in macrophages. Mol. Microbiol. 2005, 58:669-681.
    • (2005) Mol. Microbiol. , vol.58 , pp. 669-681
    • Leuzzi, R.1    Serino, L.2    Scarselli, M.3    Savino, S.4    Fontana, M.R.5    Monaci, E.6    Taddei, A.7    Fischer, G.8    Rappuoli, R.9    Pizza, M.10
  • 83
    • 84879593927 scopus 로고    scopus 로고
    • The outer surface lipoprotein VolA mediates utilization of exogenous lipids by Vibrio cholerae
    • Pride A.C., Herrera C.M., Guan Z., Giles D.K., Trent M.S. The outer surface lipoprotein VolA mediates utilization of exogenous lipids by Vibrio cholerae. MBio 2013, 4:e00305-e00313.
    • (2013) MBio , vol.4
    • Pride, A.C.1    Herrera, C.M.2    Guan, Z.3    Giles, D.K.4    Trent, M.S.5
  • 85
    • 84873633107 scopus 로고    scopus 로고
    • Lipidation of the autotransporter NalP of Neisseria meningitidis is required for its function in the release of cell-surface-exposed proteins
    • Roussel-Jazede V., Grijpstra J., van Dam V., Tommassen J., van Ulsen P. Lipidation of the autotransporter NalP of Neisseria meningitidis is required for its function in the release of cell-surface-exposed proteins. Microbiology 2013, 159:286-295.
    • (2013) Microbiology , vol.159 , pp. 286-295
    • Roussel-Jazede, V.1    Grijpstra, J.2    van Dam, V.3    Tommassen, J.4    van Ulsen, P.5
  • 87
    • 0035103994 scopus 로고    scopus 로고
    • JlpA, a novel surface-exposed lipoprotein specific to Campylobacter jejuni, mediates adherence to host epithelial cells
    • Jin S., Joe A., Lynett J., Hani E.K., Sherman P., Chan V.L. JlpA, a novel surface-exposed lipoprotein specific to Campylobacter jejuni, mediates adherence to host epithelial cells. Mol. Microbiol. 2001, 39:1225-1236.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1225-1236
    • Jin, S.1    Joe, A.2    Lynett, J.3    Hani, E.K.4    Sherman, P.5    Chan, V.L.6
  • 88
    • 84857029797 scopus 로고    scopus 로고
    • Crystal structure of JlpA, a surface-exposed lipoprotein adhesin of Campylobacter jejuni
    • Kawai F., Paek S., Choi K.J., Prouty M., Kanipes M.I., Guerry P., Yeo H.J. Crystal structure of JlpA, a surface-exposed lipoprotein adhesin of Campylobacter jejuni. J. Struct. Biol. 2012, 177:583-588.
    • (2012) J. Struct. Biol. , vol.177 , pp. 583-588
    • Kawai, F.1    Paek, S.2    Choi, K.J.3    Prouty, M.4    Kanipes, M.I.5    Guerry, P.6    Yeo, H.J.7
  • 89
    • 80051555789 scopus 로고    scopus 로고
    • The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation
    • Manfredi P., Renzi F., Mally M., Sauteur L., Schmaler M., Moes S., Jeno P., Cornelis G.R. The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation. Mol. Microbiol. 2011, 81:1050-1060.
    • (2011) Mol. Microbiol. , vol.81 , pp. 1050-1060
    • Manfredi, P.1    Renzi, F.2    Mally, M.3    Sauteur, L.4    Schmaler, M.5    Moes, S.6    Jeno, P.7    Cornelis, G.R.8
  • 91
    • 36448946927 scopus 로고    scopus 로고
    • Structure, function and transport of lipoproteins in Escherichia coli
    • ASM Press, Herndon, VA, M. Ehrmann (Ed.)
    • Tokuda H., Matsuyama S., Tanaka-Masuda K. Structure, function and transport of lipoproteins in Escherichia coli. The Periplasm 2007, 67-79. ASM Press, Herndon, VA. M. Ehrmann (Ed.).
    • (2007) The Periplasm , pp. 67-79
    • Tokuda, H.1    Matsuyama, S.2    Tanaka-Masuda, K.3
  • 92
    • 0019004444 scopus 로고
    • Outer membrane of Escherichia coli: properties of the F sex factor traT protein which is involved in surface exclusion
    • Manning P.A., Beutin L., Achtman M. Outer membrane of Escherichia coli: properties of the F sex factor traT protein which is involved in surface exclusion. J. Bacteriol. 1980, 142:285-294.
    • (1980) J. Bacteriol. , vol.142 , pp. 285-294
    • Manning, P.A.1    Beutin, L.2    Achtman, M.3
  • 93
    • 0034602835 scopus 로고    scopus 로고
    • Translocation of group 1 capsular polysaccharide to the surface of Escherichia coli requires a multimeric complex in the outer membrane
    • Drummelsmith J., Whitfield C. Translocation of group 1 capsular polysaccharide to the surface of Escherichia coli requires a multimeric complex in the outer membrane. EMBO J. 2000, 19:57-66.
    • (2000) EMBO J. , vol.19 , pp. 57-66
    • Drummelsmith, J.1    Whitfield, C.2
  • 94
    • 33645055929 scopus 로고    scopus 로고
    • Secretion of curli fibre subunits is mediated by the outer membrane-localized CsgG protein
    • Robinson L.S., Ashman E.M., Hultgren S.J., Chapman M.R. Secretion of curli fibre subunits is mediated by the outer membrane-localized CsgG protein. Mol. Microbiol. 2006, 59:870-881.
    • (2006) Mol. Microbiol. , vol.59 , pp. 870-881
    • Robinson, L.S.1    Ashman, E.M.2    Hultgren, S.J.3    Chapman, M.R.4
  • 95
    • 79951809756 scopus 로고    scopus 로고
    • The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli
    • Cowles C.E., Li Y., Semmelhack M.F., Cristea I.M., Silhavy T.J. The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli. Mol. Microbiol. 2011, 79:1168-1181.
    • (2011) Mol. Microbiol. , vol.79 , pp. 1168-1181
    • Cowles, C.E.1    Li, Y.2    Semmelhack, M.F.3    Cristea, I.M.4    Silhavy, T.J.5
  • 96
    • 84855900042 scopus 로고    scopus 로고
    • Of ticks, mice and men: understanding the dual-host lifestyle of Lyme disease spirochaetes
    • Radolf J.D., Caimano M.J., Stevenson B., Hu L.T. Of ticks, mice and men: understanding the dual-host lifestyle of Lyme disease spirochaetes. Nat. Rev. Microbiol. 2012, 10:87-99.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 87-99
    • Radolf, J.D.1    Caimano, M.J.2    Stevenson, B.3    Hu, L.T.4
  • 97
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley A.P. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 1993, 57:50-108.
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 98
    • 0025805809 scopus 로고
    • Two distinct steps in pullulanase secretion by Escherichia coli K12
    • Pugsley A.P., Poquet I., Kornacker M.G. Two distinct steps in pullulanase secretion by Escherichia coli K12. Mol. Microbiol. 1991, 5:865-873.
    • (1991) Mol. Microbiol. , vol.5 , pp. 865-873
    • Pugsley, A.P.1    Poquet, I.2    Kornacker, M.G.3
  • 99
    • 0029816618 scopus 로고    scopus 로고
    • Identification of two regions of Klebsiella oxytoca pullulanase that together are capable of promoting beta-lactamase secretion by the general secretory pathway
    • Sauvonnet N., Pugsley A.P. Identification of two regions of Klebsiella oxytoca pullulanase that together are capable of promoting beta-lactamase secretion by the general secretory pathway. Mol. Microbiol. 1996, 22:1-7.
    • (1996) Mol. Microbiol. , vol.22 , pp. 1-7
    • Sauvonnet, N.1    Pugsley, A.P.2
  • 100
    • 0031963667 scopus 로고    scopus 로고
    • The requirement for DsbA in pullulanase secretion is independent of disulphide bond formation in the enzyme
    • Sauvonnet N., Pugsley A.P. The requirement for DsbA in pullulanase secretion is independent of disulphide bond formation in the enzyme. Mol. Microbiol. 1998, 27:661-667.
    • (1998) Mol. Microbiol. , vol.27 , pp. 661-667
    • Sauvonnet, N.1    Pugsley, A.P.2
  • 101
    • 26444506255 scopus 로고    scopus 로고
    • Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca
    • Francetic O., Pugsley A.P. Towards the identification of type II secretion signals in a nonacylated variant of pullulanase from Klebsiella oxytoca. J. Bacteriol. 2005, 187:7045-7055.
    • (2005) J. Bacteriol. , vol.187 , pp. 7045-7055
    • Francetic, O.1    Pugsley, A.P.2
  • 102
    • 0025105113 scopus 로고
    • Analysis of the subcellular location of pullulanase produced by Escherichia coli carrying the pulA gene from Klebsiella pneumoniae strain UNF5023
    • Pugsley A.P., Kornacker M.G., Ryter A. Analysis of the subcellular location of pullulanase produced by Escherichia coli carrying the pulA gene from Klebsiella pneumoniae strain UNF5023. Mol. Microbiol. 1990, 4:59-72.
    • (1990) Mol. Microbiol. , vol.4 , pp. 59-72
    • Pugsley, A.P.1    Kornacker, M.G.2    Ryter, A.3
  • 103
    • 77955628595 scopus 로고    scopus 로고
    • Detailed structural and assembly model of the type II secretion pilus from sparse data
    • Campos M., Nilges M., Cisneros D.A., Francetic O. Detailed structural and assembly model of the type II secretion pilus from sparse data. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:13081-13086.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 13081-13086
    • Campos, M.1    Nilges, M.2    Cisneros, D.A.3    Francetic, O.4
  • 104
    • 0034657719 scopus 로고    scopus 로고
    • Pilus formation and protein secretion by the same machinery in Escherichia coli
    • Sauvonnet N., Vignon G., Pugsley A.P., Gounon P. Pilus formation and protein secretion by the same machinery in Escherichia coli. EMBO J. 2000, 19:2221-2228.
    • (2000) EMBO J. , vol.19 , pp. 2221-2228
    • Sauvonnet, N.1    Vignon, G.2    Pugsley, A.P.3    Gounon, P.4
  • 105
    • 0035065972 scopus 로고    scopus 로고
    • An inner membrane platform in the type II secretion machinery of Gram-negative bacteria
    • Py B., Loiseau L., Barras F. An inner membrane platform in the type II secretion machinery of Gram-negative bacteria. EMBO Rep. 2001, 2:244-248.
    • (2001) EMBO Rep. , vol.2 , pp. 244-248
    • Py, B.1    Loiseau, L.2    Barras, F.3
  • 106
    • 79955027962 scopus 로고    scopus 로고
    • Sorting of an integral outer membrane protein via the lipoprotein-specific Lol pathway and a dedicated lipoprotein pilotin
    • Collin S., Guilvout I., Nickerson N.N., Pugsley A.P. Sorting of an integral outer membrane protein via the lipoprotein-specific Lol pathway and a dedicated lipoprotein pilotin. Mol. Microbiol. 2011, 80:655-665.
    • (2011) Mol. Microbiol. , vol.80 , pp. 655-665
    • Collin, S.1    Guilvout, I.2    Nickerson, N.N.3    Pugsley, A.P.4
  • 107
    • 84878626414 scopus 로고    scopus 로고
    • The targeting, docking and anti-proteolysis functions of the secretin chaperone PulS
    • Collin S., Krehenbrink M., Guilvout I., Pugsley A.P. The targeting, docking and anti-proteolysis functions of the secretin chaperone PulS. Res. Microbiol. 2013, 164:390-396.
    • (2013) Res. Microbiol. , vol.164 , pp. 390-396
    • Collin, S.1    Krehenbrink, M.2    Guilvout, I.3    Pugsley, A.P.4
  • 108
    • 0024384953 scopus 로고
    • Klebsiella pneumoniae pulS gene encodes an outer membrane lipoprotein required for pullulanase secretion
    • D'Enfert C., Pugsley A.P. Klebsiella pneumoniae pulS gene encodes an outer membrane lipoprotein required for pullulanase secretion. J. Bacteriol. 1989, 171:3673-3679.
    • (1989) J. Bacteriol. , vol.171 , pp. 3673-3679
    • D'Enfert, C.1    Pugsley, A.P.2
  • 109
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie K.R., Lory S., Pugsley A.P. Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J. 1996, 15:978-988.
    • (1996) EMBO J. , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 110
    • 80655144742 scopus 로고    scopus 로고
    • Outer membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone
    • Nickerson N.N., Tosi T., Dessen A., Baron B., Raynal B., England P., Pugsley A.P. Outer membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone. J. Biol. Chem. 2011, 286:38833-38843.
    • (2011) J. Biol. Chem. , vol.286 , pp. 38833-38843
    • Nickerson, N.N.1    Tosi, T.2    Dessen, A.3    Baron, B.4    Raynal, B.5    England, P.6    Pugsley, A.P.7
  • 111
    • 34249825232 scopus 로고    scopus 로고
    • YaeT-independent multimerization and outer membrane association of secretin PulD
    • Collin S., Guilvout I., Chami M., Pugsley A.P. YaeT-independent multimerization and outer membrane association of secretin PulD. Mol. Microbiol. 2007, 64:1350-1357.
    • (2007) Mol. Microbiol. , vol.64 , pp. 1350-1357
    • Collin, S.1    Guilvout, I.2    Chami, M.3    Pugsley, A.P.4
  • 112
    • 0022633064 scopus 로고
    • Extracellular pullulanase of Klebsiella pneumoniae is a lipoprotein
    • Pugsley A.P., Chapon C., Schwartz M. Extracellular pullulanase of Klebsiella pneumoniae is a lipoprotein. J. Bacteriol. 1986, 166:1083-1088.
    • (1986) J. Bacteriol. , vol.166 , pp. 1083-1088
    • Pugsley, A.P.1    Chapon, C.2    Schwartz, M.3
  • 113
    • 0032726290 scopus 로고    scopus 로고
    • Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity?
    • Guilvout I., Hardie K.R., Sauvonnet N., Pugsley A.P. Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity?. J. Bacteriol. 1999, 181:7212-7220.
    • (1999) J. Bacteriol. , vol.181 , pp. 7212-7220
    • Guilvout, I.1    Hardie, K.R.2    Sauvonnet, N.3    Pugsley, A.P.4
  • 114
    • 80655125434 scopus 로고    scopus 로고
    • Determination of Borrelia surface lipoprotein anchor topology by surface proteolysis
    • Chen S., Kumru O.S., Zückert W.R. Determination of Borrelia surface lipoprotein anchor topology by surface proteolysis. J. Bacteriol. 2011, 193:6379-6383.
    • (2011) J. Bacteriol. , vol.193 , pp. 6379-6383
    • Chen, S.1    Kumru, O.S.2    Zückert, W.R.3
  • 115
    • 84886912356 scopus 로고    scopus 로고
    • Sequential steps in the assembly of the multimeric outer membrane secretin PulD
    • Huysmans G.H., Guilvout I., Pugsley A.P. Sequential steps in the assembly of the multimeric outer membrane secretin PulD. J. Biol. Chem. 2013, 288:30700-30707.
    • (2013) J. Biol. Chem. , vol.288 , pp. 30700-30707
    • Huysmans, G.H.1    Guilvout, I.2    Pugsley, A.P.3
  • 116
    • 77953924496 scopus 로고    scopus 로고
    • NalP-mediated proteolytic release of lactoferrin-binding protein B from the meningococcal cell surface
    • Roussel-Jazede V., Jongerius I., Bos M.P., Tommassen J., van Ulsen P. NalP-mediated proteolytic release of lactoferrin-binding protein B from the meningococcal cell surface. Infect. Immun. 2010, 78:3083-3089.
    • (2010) Infect. Immun. , vol.78 , pp. 3083-3089
    • Roussel-Jazede, V.1    Jongerius, I.2    Bos, M.P.3    Tommassen, J.4    van Ulsen, P.5
  • 119
    • 0026757332 scopus 로고
    • Alterations of the carboxyl-terminal amino acid residues of Escherichia coli lipoprotein affect the formation of murein-bound lipoprotein
    • Zhang W.Y., Wu H.C. Alterations of the carboxyl-terminal amino acid residues of Escherichia coli lipoprotein affect the formation of murein-bound lipoprotein. J. Biol. Chem. 1992, 267:19560-19564.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19560-19564
    • Zhang, W.Y.1    Wu, H.C.2
  • 120
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux R., Bos M.P., Geurtsen J., Mols M., Tommassen J. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 2003, 299:262-265.
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 121
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu T., Malinverni J., Ruiz N., Kim S., Silhavy T.J., Kahne D. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 2005, 121:235-245.
    • (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
  • 122
    • 84865523255 scopus 로고    scopus 로고
    • Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC
    • Webb C.T., Selkrig J., Perry A.J., Noinaj N., Buchanan S.K., Lithgow T. Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC. J. Mol. Biol. 2012, 422:545-555.
    • (2012) J. Mol. Biol. , vol.422 , pp. 545-555
    • Webb, C.T.1    Selkrig, J.2    Perry, A.J.3    Noinaj, N.4    Buchanan, S.K.5    Lithgow, T.6
  • 123
    • 73149118024 scopus 로고    scopus 로고
    • Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane
    • Ieva R., Bernstein H.D. Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:19120-19125.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 19120-19125
    • Ieva, R.1    Bernstein, H.D.2
  • 124
    • 79951813887 scopus 로고    scopus 로고
    • The double life of a bacterial lipoprotein
    • Bernstein H.D. The double life of a bacterial lipoprotein. Mol. Microbiol. 2011, 79:1128-1131.
    • (2011) Mol. Microbiol. , vol.79 , pp. 1128-1131
    • Bernstein, H.D.1
  • 125
    • 79958120924 scopus 로고    scopus 로고
    • Structure, Function and Biogenesis of the Borrelia Cell Envelope
    • Caister Academic Press, Norwich, UK, D.S. Samuels, J.D. Radolf (Eds.)
    • Bergström S., Zückert W.R. Structure, Function and Biogenesis of the Borrelia Cell Envelope. Borrelia: molecular biology, host interaction and pathogenesis 2010, 139-166. Caister Academic Press, Norwich, UK. D.S. Samuels, J.D. Radolf (Eds.).
    • (2010) Borrelia: molecular biology, host interaction and pathogenesis , pp. 139-166
    • Bergström, S.1    Zückert, W.R.2
  • 126
    • 33645077876 scopus 로고    scopus 로고
    • Borrelia burgdorferi lipoproteins are secreted to the outer surface by default
    • Schulze R.J., Zückert W.R. Borrelia burgdorferi lipoproteins are secreted to the outer surface by default. Mol. Microbiol. 2006, 59:1473-1484.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1473-1484
    • Schulze, R.J.1    Zückert, W.R.2
  • 127
    • 78049343583 scopus 로고    scopus 로고
    • Development and validation of a FACS-based lipoprotein localization screen in the Lyme disease spirochete Borrelia burgdorferi
    • Kumru O.S., Schulze R.J., Slusser J.G., Zückert W.R. Development and validation of a FACS-based lipoprotein localization screen in the Lyme disease spirochete Borrelia burgdorferi. BMC Microbiol. 2010, 10:277.
    • (2010) BMC Microbiol. , vol.10 , pp. 277
    • Kumru, O.S.1    Schulze, R.J.2    Slusser, J.G.3    Zückert, W.R.4
  • 129
    • 84855394288 scopus 로고    scopus 로고
    • Probing the Borrelia burgdorferi surface lipoprotein secretion pathway using a conditionally folding protein domain
    • Chen S., Zückert W.R. Probing the Borrelia burgdorferi surface lipoprotein secretion pathway using a conditionally folding protein domain. J. Bacteriol. 2011, 193:6724-6732.
    • (2011) J. Bacteriol. , vol.193 , pp. 6724-6732
    • Chen, S.1    Zückert, W.R.2
  • 130
    • 69249101589 scopus 로고    scopus 로고
    • Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands
    • Lilly A.A., Crane J.M., Randall L.L. Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands. Protein Sci. 2009, 18:1860-1868.
    • (2009) Protein Sci. , vol.18 , pp. 1860-1868
    • Lilly, A.A.1    Crane, J.M.2    Randall, L.L.3
  • 131
    • 0024404941 scopus 로고
    • Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein
    • Liu G., Topping T.B., Randall L.L. Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein. Proc. Natl. Acad. Sci. U. S. A. 1989, 86:9213-9217.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 9213-9217
    • Liu, G.1    Topping, T.B.2    Randall, L.L.3
  • 132
    • 0023882692 scopus 로고
    • Modulation of folding pathways of exported proteins by the leader sequence
    • Park S., Liu G., Topping T.B., Cover W.H., Randall L.L. Modulation of folding pathways of exported proteins by the leader sequence. Science 1988, 239:1033-1035.
    • (1988) Science , vol.239 , pp. 1033-1035
    • Park, S.1    Liu, G.2    Topping, T.B.3    Cover, W.H.4    Randall, L.L.5
  • 133
    • 0036809395 scopus 로고    scopus 로고
    • SecB, one small chaperone in the complex milieu of the cell
    • Randall L.L., Hardy S.J. SecB, one small chaperone in the complex milieu of the cell. Cell. Mol. Life Sci. 2002, 59:1617-1623.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1617-1623
    • Randall, L.L.1    Hardy, S.J.2
  • 134
    • 75149192610 scopus 로고    scopus 로고
    • Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins
    • Lenhart T.R., Akins D.R. Borrelia burgdorferi locus BB0795 encodes a BamA orthologue required for growth and efficient localization of outer membrane proteins. Mol. Microbiol. 2010, 75:692-709.
    • (2010) Mol. Microbiol. , vol.75 , pp. 692-709
    • Lenhart, T.R.1    Akins, D.R.2
  • 135
    • 10744223014 scopus 로고    scopus 로고
    • Cross-species surface display of functional spirochetal lipoproteins by recombinant Borrelia burgdorferi
    • Zückert W.R., Lloyd J.E., Stewart P.E., Rosa P.A., Barbour A.G. Cross-species surface display of functional spirochetal lipoproteins by recombinant Borrelia burgdorferi. Infect. Immun. 2004, 72:1463-1469.
    • (2004) Infect. Immun. , vol.72 , pp. 1463-1469
    • Zückert, W.R.1    Lloyd, J.E.2    Stewart, P.E.3    Rosa, P.A.4    Barbour, A.G.5
  • 136
    • 70349925843 scopus 로고    scopus 로고
    • Development of a single-plasmid-based regulatable gene expression system for Borrelia burgdorferi
    • Whetstine C.R., Slusser J.G., Zückert W.R. Development of a single-plasmid-based regulatable gene expression system for Borrelia burgdorferi. Appl. Environ. Microbiol. 2009, 75:6553-6558.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 6553-6558
    • Whetstine, C.R.1    Slusser, J.G.2    Zückert, W.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.