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Volumn 289, Issue 43, 2014, Pages 29457-29470

Evolutionary conservation in biogenesis of β-barrel proteins allows mitochondria to assemble a functional bacterial trimeric autotransporter protein

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOSYNTHESIS; CELL PROLIFERATION; MACHINERY; MITOCHONDRIA; YEAST;

EID: 84908266958     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.565655     Document Type: Article
Times cited : (32)

References (64)
  • 1
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal, P., Likic, V., Tachezy, J., and Lithgow, T. (2006) Evolution of the molecular machines for protein import into mitochondria. Science 313, 314-318
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 2
    • 68949207040 scopus 로고    scopus 로고
    • Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: Evolutionary conservation and divergence
    • Walther, D. M., Rapaport, D., and Tommassen, J. (2009) Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence. Cell. Mol. Life Sci. 66, 2789-2804
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2789-2804
    • Walther, D.M.1    Rapaport, D.2    Tommassen, J.3
  • 3
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the gram-negative bacterial outer membrane
    • Bos, M. P., Robert, V., and Tommassen, J. (2007) Biogenesis of the gram-negative bacterial outer membrane. Annu. Rev. Microbiol. 61, 191-214
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 4
    • 60749102331 scopus 로고    scopus 로고
    • Membrane protein architects: The role of the BAM complex in outer membrane protein assembly
    • Knowles, T. J., Scott-Tucker, A., Overduin, M., and Henderson, I. R. (2009) Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nature Rev. Microbiol. 7, 206-214
    • (2009) Nature Rev. Microbiol. , vol.7 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3    Henderson, I.R.4
  • 5
    • 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., and Tommassen, J. (2003) Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 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
  • 6
    • 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., and Kahne, D. (2005) Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 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
  • 8
    • 25144452723 scopus 로고    scopus 로고
    • Biogenesis of β-barrel membrane proteins of mitochondria
    • Paschen, S. A., Neupert, W., and Rapaport, D. (2005) Biogenesis of β-barrel membrane proteins of mitochondria. Trends Biochem. Sci. 30, 575-582
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 575-582
    • Paschen, S.A.1    Neupert, W.2    Rapaport, D.3
  • 9
    • 70349451660 scopus 로고    scopus 로고
    • Multiple pathways for mitochondrial protein traffic
    • Endo, T., and Yamano, K. (2009) Multiple pathways for mitochondrial protein traffic. Biol. Chem. 390, 723-730
    • (2009) Biol. Chem. , vol.390 , pp. 723-730
    • Endo, T.1    Yamano, K.2
  • 10
    • 0348093762 scopus 로고    scopus 로고
    • An Essential Role of Sam50 in the Protein Sorting and Assembly Machinery of the Mitochondrial Outer Membrane
    • Kozjak, V., Wiedemann, N., Milenkovic, D., Lohaus, C., Meyer, H. E., Guiard, B., Meisinger, C., and Pfanner, N. (2003) An Essential Role of Sam50 in the Protein Sorting and Assembly Machinery of the Mitochondrial Outer Membrane. J. Biol. Chem. 278, 48520-48523
    • (2003) J. Biol. Chem. , vol.278 , pp. 48520-48523
    • Kozjak, V.1    Wiedemann, N.2    Milenkovic, D.3    Lohaus, C.4    Meyer, H.E.5    Guiard, B.6    Meisinger, C.7    Pfanner, N.8
  • 12
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • Gentle, I., Gabriel, K., Beech, P., Waller, R., and Lithgow, T. (2004) The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria. J. Cell Biol. 164, 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
  • 14
    • 4444290664 scopus 로고    scopus 로고
    • Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly
    • Ishikawa, D., Yamamoto, H., Tamura, Y., Moritoh, K., and Endo, T. (2004) Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly. J. Cell Biol. 166, 621-627
    • (2004) J. Cell Biol. , vol.166 , pp. 621-627
    • Ishikawa, D.1    Yamamoto, H.2    Tamura, Y.3    Moritoh, K.4    Endo, T.5
  • 15
    • 2542499525 scopus 로고    scopus 로고
    • Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability
    • Milenkovic, D., Kozjak, V., Wiedemann, N., Lohaus, C., Meyer, H. E., Guiard, B., Pfanner, N., and Meisinger, C. (2004) Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability. J. Biol. Chem. 279, 22781-22785
    • (2004) J. Biol. Chem. , vol.279 , pp. 22781-22785
    • Milenkovic, D.1    Kozjak, V.2    Wiedemann, N.3    Lohaus, C.4    Meyer, H.E.5    Guiard, B.6    Pfanner, N.7    Meisinger, C.8
  • 17
    • 38749085210 scopus 로고    scopus 로고
    • The Peripheral Membrane Subunits of the SAM Complex Function Codependently in Mitochondrial Outer Membrane Biogenesis
    • Chan, N. C., and Lithgow, T. (2008) The Peripheral Membrane Subunits of the SAM Complex Function Codependently in Mitochondrial Outer Membrane Biogenesis. Mol. Biol. Cell 19, 126-136
    • (2008) Mol. Biol. Cell , vol.19 , pp. 126-136
    • Chan, N.C.1    Lithgow, T.2
  • 18
    • 62449307987 scopus 로고    scopus 로고
    • Signals in bacterial β-barrel proteins are functional in eukaryotic cells for targeting to and assembly in mitochondria
    • Walther, D. M., Papic, D., Bos, M. P., Tommassen, J., and Rapaport, D. (2009) Signals in bacterial β-barrel proteins are functional in eukaryotic cells for targeting to and assembly in mitochondria. Proc. Natl. Acad. Sci. U.S.A. 106, 2531-2536
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 2531-2536
    • Walther, D.M.1    Papic, D.2    Bos, M.P.3    Tommassen, J.4    Rapaport, D.5
  • 19
    • 0037090477 scopus 로고    scopus 로고
    • VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways
    • Müller, A., Rassow, J., Grimm, J., Machuy, N., Meyer, T. F., and Rudel, T. (2002) VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways. EMBO J. 21, 1916-1929
    • (2002) EMBO J. , vol.21 , pp. 1916-1929
    • Müller, A.1    Rassow, J.2    Grimm, J.3    Machuy, N.4    Meyer, T.F.5    Rudel, T.6
  • 20
    • 79960668736 scopus 로고    scopus 로고
    • Neisserial omp85 protein is selectively recognized and assembled into functional complexes in the outer membrane of human mitochondria
    • Kozjak-Pavlovic, V., Ott, C., Götz, M., and Rudel, T. (2011) Neisserial omp85 protein is selectively recognized and assembled into functional complexes in the outer membrane of human mitochondria. J. Biol. Chem. 286, 27019-27026
    • (2011) J. Biol. Chem. , vol.286 , pp. 27019-27026
    • Kozjak-Pavlovic, V.1    Ott, C.2    Götz, M.3    Rudel, T.4
  • 21
    • 77952306070 scopus 로고    scopus 로고
    • The mitochondrial porin, VDAC, has retained the ability to be assembled in the bacterial outer membrane
    • Walther, D. M., Bos, M. P., Rapaport, D., and Tommassen, J. (2010) The mitochondrial porin, VDAC, has retained the ability to be assembled in the bacterial outer membrane. Mol. Biol. Evol. 27, 887-895
    • (2010) Mol. Biol. Evol. , vol.27 , pp. 887-895
    • Walther, D.M.1    Bos, M.P.2    Rapaport, D.3    Tommassen, J.4
  • 22
    • 0034669051 scopus 로고    scopus 로고
    • Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins
    • Hoiczyk, E., Roggenkamp, A., Reichenbecher, M., Lupas, A., and Heesemann, J. (2000) Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. EMBO J. 19, 5989-5999
    • (2000) EMBO J. , vol.19 , pp. 5989-5999
    • Hoiczyk, E.1    Roggenkamp, A.2    Reichenbecher, M.3    Lupas, A.4    Heesemann, J.5
  • 23
    • 33744728321 scopus 로고    scopus 로고
    • Trimeric autotransporter adhesins: Variable structure, common function
    • Linke, D., Riess, T., Autenrieth, I. B., Lupas, A., and Kempf, V. A. (2006) Trimeric autotransporter adhesins: variable structure, common function. Trends Microbiol. 14, 264-270
    • (2006) Trends Microbiol. , vol.14 , pp. 264-270
    • Linke, D.1    Riess, T.2    Autenrieth, I.B.3    Lupas, A.4    Kempf, V.A.5
  • 24
    • 84857148914 scopus 로고    scopus 로고
    • From self sufficiency to dependence: Mechanisms and factors important for autotransporter biogenesis
    • Leyton, D. L., Rossiter, A. E., and Henderson, I. R. (2012) From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis. Nature Rev. Microbiol. 10, 213-225
    • (2012) Nature Rev. Microbiol. , vol.10 , pp. 213-225
    • Leyton, D.L.1    Rossiter, A.E.2    Henderson, I.R.3
  • 26
    • 84858226936 scopus 로고    scopus 로고
    • Type V secretion: Mechanism(s) of autotransport through the bacterial outer membrane
    • Leo, J. C., Grin, I., and Linke, D. (2012) Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane. Phil. Trans. R. Soc. B 367, 1088-1101
    • (2012) Phil. Trans. R. Soc. B , vol.367 , pp. 1088-1101
    • Leo, J.C.1    Grin, I.2    Linke, D.3
  • 30
    • 37849015898 scopus 로고    scopus 로고
    • Tetratricopeptide repeat proteins Tom70 and Tom71 mediate yeast mitochondrial morphogenesis
    • Kondo-Okamoto, N., Shaw, J. M., and Okamoto, K. (2008) Tetratricopeptide repeat proteins Tom70 and Tom71 mediate yeast mitochondrial morphogenesis. EMBO Rep. 9, 63-69
    • (2008) EMBO Rep. , vol.9 , pp. 63-69
    • Kondo-Okamoto, N.1    Shaw, J.M.2    Okamoto, K.3
  • 31
    • 0029775087 scopus 로고    scopus 로고
    • AAA proteases with catalytic sites on opposite membrane surface comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria
    • Leonhard, K., Herrmann, J. M., Stuart, R. A., Mannhaupt, G., Neupert, W., and Langer, T. (1996) AAA proteases with catalytic sites on opposite membrane surface comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria. EMBO J. 15, 4218-4229
    • (1996) EMBO J. , vol.15 , pp. 4218-4229
    • Leonhard, K.1    Herrmann, J.M.2    Stuart, R.A.3    Mannhaupt, G.4    Neupert, W.5    Langer, T.6
  • 33
    • 78349238212 scopus 로고    scopus 로고
    • C-terminal amino acid residues of the trimeric autotransporter adhesin YadA of Yersinia enterocolitica are decisive for its recognition and assembly by BamA
    • Lehr, U., Schütz, M., Oberhettinger, P., Ruiz-Perez, F., Donald, J. W., Palmer, T., Linke, D., Henderson, I. R., and Autenrieth, I. B. (2010) C-terminal amino acid residues of the trimeric autotransporter adhesin YadA of Yersinia enterocolitica are decisive for its recognition and assembly by BamA. Mol. Microbiol. 78, 932-946
    • (2010) Mol. Microbiol. , vol.78 , pp. 932-946
    • Lehr, U.1    Schütz, M.2    Oberhettinger, P.3    Ruiz-Perez, F.4    Donald, J.W.5    Palmer, T.6    Linke, D.7    Henderson, I.R.8    Autenrieth, I.B.9
  • 34
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria: Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • Daum, G., Böhni, P. C., and Schatz, G. (1982) Import of proteins into mitochondria: cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257, 13028-13033
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Böhni, P.C.2    Schatz, G.3
  • 35
    • 9244219632 scopus 로고    scopus 로고
    • Yersinia enterocolitica adhesin A induces production of interleukin-8 in epithelial cells
    • Schmid, Y., Grassl, G. A., Bühler, O. T., Skurnik, M., Autenrieth, I. B., and Bohn, E. (2004) Yersinia enterocolitica adhesin A induces production of interleukin-8 in epithelial cells. Infect. Immun. 72, 6780-6789
    • (2004) Infect. Immun. , vol.72 , pp. 6780-6789
    • Schmid, Y.1    Grassl, G.A.2    Bühler, O.T.3    Skurnik, M.4    Autenrieth, I.B.5    Bohn, E.6
  • 36
    • 33745747870 scopus 로고    scopus 로고
    • Purification of the YadA membrane anchor for secondary structure analysis and crystallization
    • Wollmann, P., Zeth, K., Lupas, A. N., and Linke, D. (2006) Purification of the YadA membrane anchor for secondary structure analysis and crystallization. Int. J. Biol. Macromol. 39, 3-9
    • (2006) Int. J. Biol. Macromol. , vol.39 , pp. 3-9
    • Wollmann, P.1    Zeth, K.2    Lupas, A.N.3    Linke, D.4
  • 38
    • 47249087402 scopus 로고    scopus 로고
    • Contribution of trimeric autotransporter C-terminal domains of oligomeric coiled-coil adhesin (Oca) family members YadA, UspA1, EibA, and Hia to translocation of the YadA passenger domain and virulence of Yersinia enterocolitica
    • Ackermann, N., Tiller, M., Anding, G., Roggenkamp, A., and Heesemann, J. (2008) Contribution of trimeric autotransporter C-terminal domains of oligomeric coiled-coil adhesin (Oca) family members YadA, UspA1, EibA, and Hia to translocation of the YadA passenger domain and virulence of Yersinia enterocolitica. J. Bacteriol. 190, 5031-5043
    • (2008) J. Bacteriol. , vol.190 , pp. 5031-5043
    • Ackermann, N.1    Tiller, M.2    Anding, G.3    Roggenkamp, A.4    Heesemann, J.5
  • 40
    • 0033606811 scopus 로고    scopus 로고
    • Biogenesis of Tom40, core component of the TOM complex of mitochondria
    • Rapaport, D., and Neupert, W. (1999) Biogenesis of Tom40, core component of the TOM complex of mitochondria. J. Cell Biol. 146, 321-331
    • (1999) J. Cell Biol. , vol.146 , pp. 321-331
    • Rapaport, D.1    Neupert, W.2
  • 43
    • 0029994354 scopus 로고    scopus 로고
    • Tom71, a novel homologue of the mitochondrial preprotein receptor Tom70
    • Schlossmann, J., Lill, R., Neupert, W., and Court, D. A. (1996) Tom71, a novel homologue of the mitochondrial preprotein receptor Tom70. J. Biol. Chem. 271, 17890-17895
    • (1996) J. Biol. Chem. , vol.271 , pp. 17890-17895
    • Schlossmann, J.1    Lill, R.2    Neupert, W.3    Court, D.A.4
  • 44
    • 0034769655 scopus 로고    scopus 로고
    • Overproduction of PDR3 suppresses mitochondrial import defects associated with a TOM70 null mutation by increasing the expression of TOM72 in Saccharomyces cerevisiae
    • Koh, J. Y., Hájek, P., and Bedwell, D. M. (2001) Overproduction of PDR3 suppresses mitochondrial import defects associated with a TOM70 null mutation by increasing the expression of TOM72 in Saccharomyces cerevisiae. Mol. Cell Biol. 21, 7576-7586
    • (2001) Mol. Cell Biol. , vol.21 , pp. 7576-7586
    • Koh, J.Y.1    Hájek, P.2    Bedwell, D.M.3
  • 45
    • 80052579096 scopus 로고    scopus 로고
    • Multispan mitochondrial outer membrane protein Ugo1 follows a unique Mim1-dependent import pathway
    • Papic, D., Krumpe, K., Dukanovic, J., Dimmer, K. S., and Rapaport, D. (2011) Multispan mitochondrial outer membrane protein Ugo1 follows a unique Mim1-dependent import pathway. J. Cell Biol. 194, 397-405
    • (2011) J. Cell Biol. , vol.194 , pp. 397-405
    • Papic, D.1    Krumpe, K.2    Dukanovic, J.3    Dimmer, K.S.4    Rapaport, D.5
  • 46
    • 0033544854 scopus 로고    scopus 로고
    • Biogenesis of Mitochondrial Inner Membrane Proteins
    • Tokatlidis, K., and Schatz, G. (1999) Biogenesis of Mitochondrial Inner Membrane Proteins. J. Biol. Chem. 274, 35285-35288
    • (1999) J. Biol. Chem. , vol.274 , pp. 35285-35288
    • Tokatlidis, K.1    Schatz, G.2
  • 47
    • 0346687594 scopus 로고    scopus 로고
    • The small Tim proteins and the twin Cx3C motif
    • Koehler, C. M. (2004) The small Tim proteins and the twin Cx3C motif. Trends Biochem. Sci 29, 1-4
    • (2004) Trends Biochem. Sci , vol.29 , pp. 1-4
    • Koehler, C.M.1
  • 48
    • 84865025618 scopus 로고    scopus 로고
    • Chloroplast β-barrel proteins are assembled into the mitochondrial outer membrane in a process that depends on the TOM and TOB complexes
    • Ulrich, T., Gross, L. E., Sommer, M. S., Schleiff, E., and Rapaport, D. (2012) Chloroplast β-barrel proteins are assembled into the mitochondrial outer membrane in a process that depends on the TOM and TOB complexes. J. Biol. Chem. 287, 27467-27479
    • (2012) J. Biol. Chem. , vol.287 , pp. 27467-27479
    • Ulrich, T.1    Gross, L.E.2    Sommer, M.S.3    Schleiff, E.4    Rapaport, D.5
  • 49
    • 0036809395 scopus 로고    scopus 로고
    • SecB, one small chaperone in the complex milieu of the cell
    • Randall, L. L., and Hardy, S. J. (2002) SecB, one small chaperone in the complex milieu of the cell. Cell Mol. Life Sci. 59, 1617-1623
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 1617-1623
    • Randall, L.L.1    Hardy, S.J.2
  • 51
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
    • Sklar, J. G., Wu, T., Kahne, D., and Silhavy, T. J. (2007) Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev. 21, 2473-2484
    • (2007) Genes Dev. , vol.21 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 52
    • 38749106998 scopus 로고    scopus 로고
    • Conserved substrate binding by chaperones in the bacterial periplasm and the mitochondrial intermembrane space
    • Alcock, F. H., Grossmann, J. G., Gentle, I. E., Likić, V. A., Lithgow, T., and Tokatlidis, K. (2008) Conserved substrate binding by chaperones in the bacterial periplasm and the mitochondrial intermembrane space. Biochem. J. 409, 377-387
    • (2008) Biochem. J. , vol.409 , pp. 377-387
    • Alcock, F.H.1    Grossmann, J.G.2    Gentle, I.E.3    Likić, V.A.4    Lithgow, T.5    Tokatlidis, K.6
  • 53
    • 2142710081 scopus 로고    scopus 로고
    • Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor
    • Herlan, M., Bornhövd, C., Hell, K., Neupert, W., and Reichert, A. S. (2004) Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor. J. Cell Biol. 165, 167-173
    • (2004) J. Cell Biol. , vol.165 , pp. 167-173
    • Herlan, M.1    Bornhövd, C.2    Hell, K.3    Neupert, W.4    Reichert, A.S.5
  • 54
    • 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
    • Qu, J., Mayer, C., Behrens, S., Holst, O., and Kleinschmidt, J. H. (2007) 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, 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
  • 55
    • 0033602381 scopus 로고    scopus 로고
    • Chaperonelike activity of the AAA domain of the yeast Yme1 AAA protease
    • Leonhard, K., Stiegler, A., Neupert, W., and Langer, T. (1999) Chaperonelike activity of the AAA domain of the yeast Yme1 AAA protease. Nature 398, 348-351
    • (1999) Nature , vol.398 , pp. 348-351
    • Leonhard, K.1    Stiegler, A.2    Neupert, W.3    Langer, T.4
  • 56
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer, T., Sawa, J., Schäfer, E., Saibil, H. R., Ehrmann, M., and Clausen, T. (2008) Structural basis for the regulated protease and chaperone function of DegP. Nature 453, 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
  • 57
    • 60549101514 scopus 로고    scopus 로고
    • The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains
    • Walton, T. A., Sandoval, C. M., Fowler, C. A., Pardi, A., and Sousa, M. C. (2009) The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc. Natl. Acad. Sci. U.S.A. 106, 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
  • 58
    • 79961225871 scopus 로고    scopus 로고
    • Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain
    • Ieva, R., Tian, P., Peterson, J. H., and Bernstein, H. D. (2011) Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain. Proc. Natl. Acad. Sci. U.S.A. 108, 383-391
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 383-391
    • Ieva, R.1    Tian, P.2    Peterson, J.H.3    Bernstein, H.D.4
  • 59
    • 79952789687 scopus 로고    scopus 로고
    • Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis
    • Volokhina, E. B., Grijpstra, J., Stork, M., Schilders, I., Tommassen, J., and Bos, M. P. (2011) Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis. J. Bacteriol. 193, 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
  • 61
    • 80052966272 scopus 로고    scopus 로고
    • Autotransporter beta-domains have a specific function in protein secretion beyond outer-membrane targeting
    • Saurí, A., Oreshkova, N., Soprova, Z., Jong, W. S., Sani, M., Peters, P. J., Luirink, J., and van Ulsen, P. (2011) Autotransporter beta-domains have a specific function in protein secretion beyond outer-membrane targeting. J. Mol. Biol. 412, 553-567
    • (2011) J. Mol. Biol. , vol.412 , pp. 553-567
    • Saurí, A.1    Oreshkova, N.2    Soprova, Z.3    Jong, W.S.4    Sani, M.5    Peters, P.J.6    Luirink, J.7    Van Ulsen, P.8
  • 62
    • 84874594746 scopus 로고    scopus 로고
    • Mechanistic link between beta barrel assembly and the initiation of autotransporter secretion
    • Pavlova, O., Peterson, J. H., Ieva, R., and Bernstein, H. D. (2013) Mechanistic link between beta barrel assembly and the initiation of autotransporter secretion. Proc. Natl. Acad. Sci. U.S.A. 110, 938-947
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 938-947
    • Pavlova, O.1    Peterson, J.H.2    Ieva, R.3    Bernstein, H.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.