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Volumn 403, Issue 2, 2010, Pages 270-285

TolA Modulates the Oligomeric Status of YbgF in the Bacterial Periplasm

Author keywords

Outer membrane; Periplasm; Protein protein interaction; Quaternary structure; Tol Pal complex

Indexed keywords

BACTERIAL PROTEIN; PERIPLASMIC PROTEIN; PROTEIN TOL A; PROTEIN YBGF; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; MEMBRANE PROTEIN; PROTEIN BINDING; TOLA PROTEIN, E COLI; TOLB PROTEIN, E COLI; YBGF PROTEIN, E COLI;

EID: 77957234943     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.08.050     Document Type: Article
Times cited : (32)

References (29)
  • 1
    • 33846650968 scopus 로고    scopus 로고
    • The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli
    • Gerding M.A., Ogata Y., Pecora N.D., Niki H., de Boer P.A. The trans-envelope Tol-Pal complex is part of the cell division machinery and required for proper outer-membrane invagination during cell constriction in E. coli. Mol. Microbiol. 2007, 63:1008-1025.
    • (2007) Mol. Microbiol. , vol.63 , pp. 1008-1025
    • Gerding, M.A.1    Ogata, Y.2    Pecora, N.D.3    Niki, H.4    de Boer, P.A.5
  • 2
    • 0019473245 scopus 로고
    • Genetic and biochemical characterization of periplasmic-leaky mutants of Escherichia coli K-12
    • Lazzaroni J.C., Portalier R.C. Genetic and biochemical characterization of periplasmic-leaky mutants of Escherichia coli K-12. J. Bacteriol. 1981, 145:1351-1358.
    • (1981) J. Bacteriol. , vol.145 , pp. 1351-1358
    • Lazzaroni, J.C.1    Portalier, R.C.2
  • 3
    • 0015416336 scopus 로고
    • Pleiotropic properties and genetic organization of the tolA,B locus of Escherichia coli K-12
    • Bernstein A., Rolfe B., Onodera K. Pleiotropic properties and genetic organization of the tolA,B locus of Escherichia coli K-12. J. Bacteriol. 1972, 112:74-83.
    • (1972) J. Bacteriol. , vol.112 , pp. 74-83
    • Bernstein, A.1    Rolfe, B.2    Onodera, K.3
  • 4
    • 61449198592 scopus 로고    scopus 로고
    • Deletion of tolA in Salmonella Typhimurium generates an attenuated strain with vaccine potential
    • Paterson G.K., Northen H., Cone D.B., Willers C., Peters S.E., Maskell D.J. Deletion of tolA in Salmonella Typhimurium generates an attenuated strain with vaccine potential. Microbiology 2009, 155:220-228.
    • (2009) Microbiology , vol.155 , pp. 220-228
    • Paterson, G.K.1    Northen, H.2    Cone, D.B.3    Willers, C.4    Peters, S.E.5    Maskell, D.J.6
  • 5
    • 0033303795 scopus 로고    scopus 로고
    • Impairment of cell division in tolA mutants of Escherichia coli at low and high medium osmolarities
    • Meury J., Devilliers G. Impairment of cell division in tolA mutants of Escherichia coli at low and high medium osmolarities. Biol. Cell 1999, 91:67-75.
    • (1999) Biol. Cell , vol.91 , pp. 67-75
    • Meury, J.1    Devilliers, G.2
  • 6
    • 0014137931 scopus 로고
    • Genetics and physiology of colicin-tolerant mutants of Escherichia coli
    • Nagel de Zwaig R., Luria S.E. Genetics and physiology of colicin-tolerant mutants of Escherichia coli. J. Bacteriol. 1967, 94:1112-1123.
    • (1967) J. Bacteriol. , vol.94 , pp. 1112-1123
    • Nagel de Zwaig, R.1    Luria, S.E.2
  • 7
    • 0030797114 scopus 로고    scopus 로고
    • The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli
    • Riechmann L., Holliger P. The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli. Cell 1997, 90:351-360.
    • (1997) Cell , vol.90 , pp. 351-360
    • Riechmann, L.1    Holliger, P.2
  • 8
    • 0036589166 scopus 로고    scopus 로고
    • The Tol proteins of Escherichia coli and their involvement in the translocation of group A colicins
    • Lazzaroni J.C., Dubuisson J.F., Vianney A. The Tol proteins of Escherichia coli and their involvement in the translocation of group A colicins. Biochimie 2002, 84:391-397.
    • (2002) Biochimie , vol.84 , pp. 391-397
    • Lazzaroni, J.C.1    Dubuisson, J.F.2    Vianney, A.3
  • 9
    • 0029055749 scopus 로고
    • Protein complex within Escherichia coli inner membrane. TolA N-terminal domain interacts with TolQ and TolR proteins
    • Derouiche R., Benedetti H., Lazzaroni J.C., Lazdunski C., Lloubes R. Protein complex within Escherichia coli inner membrane. TolA N-terminal domain interacts with TolQ and TolR proteins. J. Biol. Chem. 1995, 270:11078-11084.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11078-11084
    • Derouiche, R.1    Benedetti, H.2    Lazzaroni, J.C.3    Lazdunski, C.4    Lloubes, R.5
  • 10
    • 0029045244 scopus 로고
    • Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli
    • Bouveret E., Derouiche R., Rigal A., Lloubes R., Lazdunski C., Benedetti H. Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli. J. Biol. Chem. 1995, 270:11071-11077.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11071-11077
    • Bouveret, E.1    Derouiche, R.2    Rigal, A.3    Lloubes, R.4    Lazdunski, C.5    Benedetti, H.6
  • 11
    • 70349205369 scopus 로고    scopus 로고
    • Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins
    • Bonsor D.A., Hecht O., Vankemmelbeke M., Sharma A., Krachler A.M., Housden N.G., et al. Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins. EMBO J. 2009, 28:2846-2857.
    • (2009) EMBO J. , vol.28 , pp. 2846-2857
    • Bonsor, D.A.1    Hecht, O.2    Vankemmelbeke, M.3    Sharma, A.4    Krachler, A.M.5    Housden, N.G.6
  • 12
    • 8944230187 scopus 로고    scopus 로고
    • Characterization of the tol-pal region of Escherichia coli K-12: translational control of tolR expression by TolQ and identification of a new open reading frame downstream of pal encoding a periplasmic protein
    • Vianney A., Muller M.M., Clavel T., Lazzaroni J.C., Portalier R., Webster R.E. Characterization of the tol-pal region of Escherichia coli K-12: translational control of tolR expression by TolQ and identification of a new open reading frame downstream of pal encoding a periplasmic protein. J. Bacteriol. 1996, 178:4031-4038.
    • (1996) J. Bacteriol. , vol.178 , pp. 4031-4038
    • Vianney, A.1    Muller, M.M.2    Clavel, T.3    Lazzaroni, J.C.4    Portalier, R.5    Webster, R.E.6
  • 13
    • 0035155704 scopus 로고    scopus 로고
    • Organisation and evolution of the tol-pal gene cluster
    • Sturgis J.N. Organisation and evolution of the tol-pal gene cluster. J. Mol. Microbiol. Biotechnol. 2001, 3:113-122.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 113-122
    • Sturgis, J.N.1
  • 14
    • 0037051944 scopus 로고    scopus 로고
    • The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis
    • Zhuang Z., Song F., Martin B.M., Dunaway-Mariano D. The YbgC protein encoded by the ybgC gene of the tol-pal gene cluster of Haemophilus influenzae catalyzes acyl-coenzyme A thioester hydrolysis. FEBS Lett. 2002, 516:161-163.
    • (2002) FEBS Lett. , vol.516 , pp. 161-163
    • Zhuang, Z.1    Song, F.2    Martin, B.M.3    Dunaway-Mariano, D.4
  • 15
    • 0036093944 scopus 로고    scopus 로고
    • The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB
    • Walburger A., Lazdunski C., Corda Y. The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB. Mol. Microbiol. 2002, 44:695-708.
    • (2002) Mol. Microbiol. , vol.44 , pp. 695-708
    • Walburger, A.1    Lazdunski, C.2    Corda, Y.3
  • 16
    • 77953593958 scopus 로고    scopus 로고
    • Self-association of TPR domains: lessons learned from a designed, consensus-based TPR oligomer
    • Krachler A.M., Sharma A., Kleanthous C. Self-association of TPR domains: lessons learned from a designed, consensus-based TPR oligomer. Proteins 2010, 78:2131-2143.
    • (2010) Proteins , vol.78 , pp. 2131-2143
    • Krachler, A.M.1    Sharma, A.2    Kleanthous, C.3
  • 17
    • 0036330840 scopus 로고    scopus 로고
    • Mutational analysis of the TolA C-terminal domain of Escherichia coli and genetic evidence for an interaction between TolA and TolB
    • Dubuisson J.F., Vianney A., Lazzaroni J.C. Mutational analysis of the TolA C-terminal domain of Escherichia coli and genetic evidence for an interaction between TolA and TolB. J. Bacteriol. 2002, 184:4620-4625.
    • (2002) J. Bacteriol. , vol.184 , pp. 4620-4625
    • Dubuisson, J.F.1    Vianney, A.2    Lazzaroni, J.C.3
  • 19
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P.B., Zhang T., Kim P.S., Alber T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 1993, 262:1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 22
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 23
    • 52649130704 scopus 로고    scopus 로고
    • Protein-protein interaction and quaternary structure
    • Janin J., Bahadur R.P., Chakrabarti P. Protein-protein interaction and quaternary structure. Q. Rev. Biophys. 2008, 41:133-180.
    • (2008) Q. Rev. Biophys. , vol.41 , pp. 133-180
    • Janin, J.1    Bahadur, R.P.2    Chakrabarti, P.3
  • 24
    • 4344575287 scopus 로고    scopus 로고
    • Coiled coil domains: stability, specificity, and biological implications
    • Mason J.M., Arndt K.M. Coiled coil domains: stability, specificity, and biological implications. ChemBioChem 2004, 5:170-176.
    • (2004) ChemBioChem , vol.5 , pp. 170-176
    • Mason, J.M.1    Arndt, K.M.2
  • 25
    • 0025912823 scopus 로고
    • TolA: a membrane protein involved in colicin uptake contains an extended helical region
    • Levengood S.K., Beyer W.F., Webster R.E. TolA: a membrane protein involved in colicin uptake contains an extended helical region. Proc. Natl Acad. Sci. USA 1991, 88:5939-5943.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5939-5943
    • Levengood, S.K.1    Beyer, W.F.2    Webster, R.E.3
  • 26
    • 0033637616 scopus 로고    scopus 로고
    • Proton motive force drives the interaction of the inner membrane TolA and outer membrane pal proteins in Escherichia coli
    • Cascales E., Gavioli M., Sturgis J.N., Lloubes R. Proton motive force drives the interaction of the inner membrane TolA and outer membrane pal proteins in Escherichia coli. Mol. Microbiol. 2000, 38:904-915.
    • (2000) Mol. Microbiol. , vol.38 , pp. 904-915
    • Cascales, E.1    Gavioli, M.2    Sturgis, J.N.3    Lloubes, R.4
  • 27
    • 0034944420 scopus 로고    scopus 로고
    • The Tol-Pal proteins of the Escherichia coli cell envelope: an energized system required for outer membrane integrity?
    • Lloubes R., Cascales E., Walburger A., Bouveret E., Lazdunski C., Bernadac A., Journet L. The Tol-Pal proteins of the Escherichia coli cell envelope: an energized system required for outer membrane integrity?. Res. Microbiol. 2001, 152:523-529.
    • (2001) Res. Microbiol. , vol.152 , pp. 523-529
    • Lloubes, R.1    Cascales, E.2    Walburger, A.3    Bouveret, E.4    Lazdunski, C.5    Bernadac, A.6    Journet, L.7
  • 28
    • 0037648552 scopus 로고    scopus 로고
    • Design of stable alpha-helical arrays from an idealized TPR motif
    • Main E.R., Xiong Y., Cocco M.J., D'Andrea L., Regan L. Design of stable alpha-helical arrays from an idealized TPR motif. Structure 2003, 11:497-508.
    • (2003) Structure , vol.11 , pp. 497-508
    • Main, E.R.1    Xiong, Y.2    Cocco, M.J.3    D'Andrea, L.4    Regan, L.5
  • 29
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 2000, 78:1606-1619.
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.