메뉴 건너뛰기




Volumn 52, Issue 35, 2013, Pages 6108-6113

Bam lipoproteins assemble BamA in vitro

Author keywords

[No Author keywords available]

Indexed keywords

CENTRAL COMPONENT; GRAM-NEGATIVE BACTERIA; IN-VITRO; IN-VITRO ASSAYS; MEMBRANE PROTEINS; OUTER MEMBRANE; SPECIFIC COMPONENT;

EID: 84883468908     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400865z     Document Type: Article
Times cited : (57)

References (35)
  • 1
    • 50649104037 scopus 로고    scopus 로고
    • Protein translocation across the bacterial cytoplasmic membrane
    • Driessen, A. J. and Nouwen, N. (2008) Protein translocation across the bacterial cytoplasmic membrane Annu. Rev. Biochem. 77, 643-667
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 643-667
    • Driessen, A.J.1    Nouwen, N.2
  • 2
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P. and Johnson, A. E. (1994) Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane Annu. Rev. Cell Biol. 10, 87-119
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 3
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport, T. A. (2007) Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes Nature 450, 663-669
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 4
    • 79959468179 scopus 로고    scopus 로고
    • β-Barrel Membrane Protein Assembly by the Bam Complex
    • Hagan, C. L., Silhavy, T. J., and Kahne, D. (2011) β-Barrel Membrane Protein Assembly by the Bam Complex Annu. Rev. Biochem. 80, 189-210
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 189-210
    • Hagan, C.L.1    Silhavy, T.J.2    Kahne, D.3
  • 5
    • 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
  • 6
    • 33745202589 scopus 로고    scopus 로고
    • YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
    • Malinverni, J. C., Werner, J., Kim, S., Sklar, J. G., Kahne, D., Misra, R., and Silhavy, T. J. (2006) YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli Mol. Microbiol. 61, 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
  • 7
    • 34548139422 scopus 로고    scopus 로고
    • Structure and function of an essential component of the outer membrane protein assembly machine
    • Kim, S., Malinverni, J. C., Sliz, P., Silhavy, T. J., Harrison, S. C., and Kahne, D. (2007) Structure and function of an essential component of the outer membrane protein assembly machine Science 317, 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
  • 8
    • 0035850868 scopus 로고    scopus 로고
    • Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin
    • Eggert, U. S., Ruiz, N., Falcone, B. V., Branstrom, A. A., Goldman, R. C., Silhavy, T. J., and Kahne, D. (2001) Genetic basis for activity differences between vancomycin and glycolipid derivatives of vancomycin Science 294, 361-364
    • (2001) Science , vol.294 , pp. 361-364
    • Eggert, U.S.1    Ruiz, N.2    Falcone, B.V.3    Branstrom, A.A.4    Goldman, R.C.5    Silhavy, T.J.6    Kahne, D.7
  • 9
    • 17444385981 scopus 로고    scopus 로고
    • Chemical conditionality: A genetic strategy to probe organelle assembly
    • Ruiz, N., Falcone, B., Kahne, D., and Silhavy, T. J. (2005) Chemical conditionality: A genetic strategy to probe organelle assembly Cell 121, 307-317
    • (2005) Cell , vol.121 , pp. 307-317
    • Ruiz, N.1    Falcone, B.2    Kahne, D.3    Silhavy, T.J.4
  • 10
    • 34547512065 scopus 로고    scopus 로고
    • Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli
    • Sklar, J. G., Wu, T., Gronenberg, L. S., Malinverni, J. C., Kahne, D., and Silhavy, T. J. (2007) 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, 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
  • 11
    • 0033582158 scopus 로고    scopus 로고
    • The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: Identification of a cyanobacterial homolog
    • Reumann, S., Davila-Aponte, J., and Keegstra, K. (1999) The evolutionary origin of the protein-translocating channel of chloroplastic envelope membranes: Identification of a cyanobacterial homolog Proc. Natl. Acad. Sci. U.S.A. 96, 784-789
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 784-789
    • Reumann, S.1    Davila-Aponte, J.2    Keegstra, K.3
  • 12
    • 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
  • 15
    • 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
  • 16
    • 55549098175 scopus 로고    scopus 로고
    • The Omp85-related chloroplast outer envelope protein OEP80 is essential for viability in Arabidopsis
    • Patel, R., Hsu, S. C., Bedard, J., Inoue, K., and Jarvis, P. (2008) The Omp85-related chloroplast outer envelope protein OEP80 is essential for viability in Arabidopsis Plant Physiol. 148, 235-245
    • (2008) Plant Physiol. , vol.148 , pp. 235-245
    • Patel, R.1    Hsu, S.C.2    Bedard, J.3    Inoue, K.4    Jarvis, P.5
  • 17
    • 77952363712 scopus 로고    scopus 로고
    • Reconstitution of outer membrane protein assembly from purified components
    • Hagan, C. L., Kim, S., and Kahne, D. (2010) Reconstitution of outer membrane protein assembly from purified components Science 328, 890-892
    • (2010) Science , vol.328 , pp. 890-892
    • Hagan, C.L.1    Kim, S.2    Kahne, D.3
  • 18
    • 80052232601 scopus 로고    scopus 로고
    • The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of β-barrel assembly
    • Hagan, C. L. and Kahne, D. (2011) The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of β-barrel assembly Biochemistry 50, 7444-7446
    • (2011) Biochemistry , vol.50 , pp. 7444-7446
    • Hagan, C.L.1    Kahne, D.2
  • 19
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar, S. W. and Kolter, R. (1996) SurA assists the folding of Escherichia coli outer membrane proteins J. Bacteriol. 178, 1770-1773
    • (1996) J. Bacteriol. , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 20
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouviere, P. E. and Gross, C. A. (1996) SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins Genes Dev. 10, 3170-3182
    • (1996) Genes Dev. , vol.10 , pp. 3170-3182
    • Rouviere, P.E.1    Gross, C.A.2
  • 21
    • 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
  • 22
    • 66249114348 scopus 로고    scopus 로고
    • Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics
    • Vertommen, D., Ruiz, N., Leverrier, P., Silhavy, T. J., and Collet, J. F. (2009) Characterization of the role of the Escherichia coli periplasmic chaperone SurA using differential proteomics Proteomics 9, 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
  • 23
    • 77956153485 scopus 로고    scopus 로고
    • Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli
    • Bennion, D., Charlson, E. S., Coon, E., and Misra, R. (2010) Dissection of β-barrel outer membrane protein assembly pathways through characterizing BamA POTRA 1 mutants of Escherichia coli Mol. Microbiol. 77, 1153-1171
    • (2010) Mol. Microbiol. , vol.77 , pp. 1153-1171
    • Bennion, D.1    Charlson, E.S.2    Coon, E.3    Misra, R.4
  • 24
    • 84855886701 scopus 로고    scopus 로고
    • Substitutions in the BamA β-barrel domain overcome the conditional lethal phenotype of a Δ bamB Δ bamE strain of Escherichia coli
    • Tellez, R., Jr. and Misra, R. (2011) Substitutions in the BamA β-barrel domain overcome the conditional lethal phenotype of a Δ bamB Δ bamE strain of Escherichia coli J. Bacteriol. 194, 317-324
    • (2011) J. Bacteriol. , vol.194 , pp. 317-324
    • Tellez Jr., R.1    Misra, R.2
  • 25
    • 84861172996 scopus 로고    scopus 로고
    • Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics
    • Denoncin, K., Schwalm, J., Vertommen, D., Silhavy, T. J., and Collet, J. F. (2012) Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics Proteomics 12, 1391-1401
    • (2012) Proteomics , vol.12 , pp. 1391-1401
    • Denoncin, K.1    Schwalm, J.2    Vertommen, D.3    Silhavy, T.J.4    Collet, J.F.5
  • 26
    • 84878935527 scopus 로고    scopus 로고
    • The Lipid Bilayer-Inserted Membrane Protein BamA of Escherichia coli Facilitates Insertion and Folding of Outer Membrane Protein A from Its Complex with Skp
    • Patel, G. J. and Kleinschmidt, J. H. (2013) The Lipid Bilayer-Inserted Membrane Protein BamA of Escherichia coli Facilitates Insertion and Folding of Outer Membrane Protein A from Its Complex with Skp Biochemistry 52, 3974-3986
    • (2013) Biochemistry , vol.52 , pp. 3974-3986
    • Patel, G.J.1    Kleinschmidt, J.H.2
  • 27
    • 79952311132 scopus 로고    scopus 로고
    • The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex
    • Noinaj, N., Fairman, J. W., and Buchanan, S. K. (2011) The crystal structure of BamB suggests interactions with BamA and its role within the BAM complex J. Mol. Biol. 407, 248-260
    • (2011) J. Mol. Biol. , vol.407 , pp. 248-260
    • Noinaj, N.1    Fairman, J.W.2    Buchanan, S.K.3
  • 28
    • 79960974503 scopus 로고    scopus 로고
    • Structural basis of outer membrane protein biogenesis in bacteria
    • Albrecht, R. and Zeth, K. (2011) Structural basis of outer membrane protein biogenesis in bacteria J. Biol. Chem. 286, 27792-27803
    • (2011) J. Biol. Chem. , vol.286 , pp. 27792-27803
    • Albrecht, R.1    Zeth, K.2
  • 29
    • 79951769354 scopus 로고    scopus 로고
    • Augmenting β-augmentation: Structural basis of how BamB binds BamA and may support folding of outer membrane proteins
    • Heuck, A., Schleiffer, A., and Clausen, T. (2011) Augmenting β-augmentation: Structural basis of how BamB binds BamA and may support folding of outer membrane proteins J. Mol. Biol. 406, 659-666
    • (2011) J. Mol. Biol. , vol.406 , pp. 659-666
    • Heuck, A.1    Schleiffer, A.2    Clausen, T.3
  • 30
    • 79956148245 scopus 로고    scopus 로고
    • Crystal Structure of BamD: An Essential Component of the β-Barrel Assembly Machinery of Gram-Negative Bacteria
    • Sandoval, C. M., Baker, S. L., Jansen, K., Metzner, S. I., and Sousa, M. C. (2011) Crystal Structure of BamD: An Essential Component of the β-Barrel Assembly Machinery of Gram-Negative Bacteria J. Mol. Biol. 409, 348-357
    • (2011) J. Mol. Biol. , vol.409 , pp. 348-357
    • Sandoval, C.M.1    Baker, S.L.2    Jansen, K.3    Metzner, S.I.4    Sousa, M.C.5
  • 31
    • 79951772443 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli BamB, a lipoprotein component of the β-barrel assembly machinery complex
    • Kim, K. H. and Paetzel, M. (2011) Crystal structure of Escherichia coli BamB, a lipoprotein component of the β-barrel assembly machinery complex J. Mol. Biol. 406, 667-678
    • (2011) J. Mol. Biol. , vol.406 , pp. 667-678
    • Kim, K.H.1    Paetzel, M.2
  • 32
    • 80655149463 scopus 로고    scopus 로고
    • Crystal structure of β-barrel assembly machinery BamCD protein complex
    • Kim, K. H., Aulakh, S., and Paetzel, M. (2011) Crystal structure of β-barrel assembly machinery BamCD protein complex J. Biol. Chem. 286, 39116-39121
    • (2011) J. Biol. Chem. , vol.286 , pp. 39116-39121
    • Kim, K.H.1    Aulakh, S.2    Paetzel, M.3
  • 33
    • 79961225871 scopus 로고    scopus 로고
    • Sequential and spatially restricted interactions of assembly factors with an autotransporter β domain
    • Ieva, R., Tian, P., Peterson, J. H., and Bernstein, H. D. (2011) Sequential and spatially restricted interactions of assembly factors with an autotransporter β domain Proc. Natl. Acad. Sci. U.S.A. 108, E383-E391
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108
    • Ieva, R.1    Tian, P.2    Peterson, J.H.3    Bernstein, H.D.4
  • 34
    • 33646727775 scopus 로고    scopus 로고
    • Folding kinetics of the outer membrane proteins OmpA and FomA into phospholipid bilayers
    • Kleinschmidt, J. H. (2006) Folding kinetics of the outer membrane proteins OmpA and FomA into phospholipid bilayers Chem. Phys. Lipids 141, 30-47
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 30-47
    • Kleinschmidt, J.H.1
  • 35
    • 55549120907 scopus 로고    scopus 로고
    • β-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro
    • Burgess, N. K., Dao, T. P., Stanley, A. M., and Fleming, K. G. (2008) β-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro J. Biol. Chem. 283, 26748-26758
    • (2008) J. Biol. Chem. , vol.283 , pp. 26748
    • Burgess, N.K.1    Dao, T.P.2    Stanley, A.M.3    Fleming, K.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.