메뉴 건너뛰기




Volumn 581, Issue 21, 2007, Pages 4085-4090

The TatBC complex formation suppresses a modular TatB-multimerization in Escherichia coli

Author keywords

Membrane protein complexes; Protein transport; Translocon assembly; Twin arginine translocation

Indexed keywords

OUTER MEMBRANE PROTEIN; TATA PROTEIN; TATB PROTEIN; TATC PROTEIN; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 34547699063     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.07.045     Document Type: Article
Times cited : (30)

References (20)
  • 1
    • 15744405122 scopus 로고    scopus 로고
    • Protein targeting by the bacterial twin-arginine translocation (Tat) pathway
    • Berks B.C., Palmer T., and Sargent F. Protein targeting by the bacterial twin-arginine translocation (Tat) pathway. Curr. Opin. Microbiol. 8 (2005) 174-181
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 174-181
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 2
    • 14644395585 scopus 로고    scopus 로고
    • Twin-arginine-specific protein export in Escherichia coli
    • Müller M. Twin-arginine-specific protein export in Escherichia coli. Res. Microbiol. 156 (2005) 131-136
    • (2005) Res. Microbiol. , vol.156 , pp. 131-136
    • Müller, M.1
  • 3
    • 0036276602 scopus 로고    scopus 로고
    • Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system
    • Yen M.R., Tseng Y.H., Nguyen E.H., Wu L.F., and Saier Jr. M.H. Sequence and phylogenetic analyses of the twin-arginine targeting (Tat) protein export system. Arch. Microbiol. 177 (2002) 441-450
    • (2002) Arch. Microbiol. , vol.177 , pp. 441-450
    • Yen, M.R.1    Tseng, Y.H.2    Nguyen, E.H.3    Wu, L.F.4    Saier Jr., M.H.5
  • 4
    • 0035812905 scopus 로고    scopus 로고
    • Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway
    • de Leeuw E., Porcelli I., Sargent F., Palmer T., and Berks B.C. Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway. FEBS Lett. 506 (2001) 143-148
    • (2001) FEBS Lett. , vol.506 , pp. 143-148
    • de Leeuw, E.1    Porcelli, I.2    Sargent, F.3    Palmer, T.4    Berks, B.C.5
  • 5
    • 12344296658 scopus 로고    scopus 로고
    • The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex
    • Oates J., Barrett C.M., Barnett J.P., Byrne K.G., Bolhuis A., and Robinson C. The Escherichia coli twin-arginine translocation apparatus incorporates a distinct form of TatABC complex, spectrum of modular TatA complexes and minor TatAB complex. J. Mol. Biol. 346 (2005) 295-305
    • (2005) J. Mol. Biol. , vol.346 , pp. 295-305
    • Oates, J.1    Barrett, C.M.2    Barnett, J.P.3    Byrne, K.G.4    Bolhuis, A.5    Robinson, C.6
  • 6
    • 30044442673 scopus 로고    scopus 로고
    • Targeting of unfolded PhoA to the TAT translocon of Escherichia coli
    • Richter S., and Brüser T. Targeting of unfolded PhoA to the TAT translocon of Escherichia coli. J. Biol. Chem. 280 (2005) 42723-42730
    • (2005) J. Biol. Chem. , vol.280 , pp. 42723-42730
    • Richter, S.1    Brüser, T.2
  • 7
    • 33646837543 scopus 로고    scopus 로고
    • Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport
    • Dabney-Smith C., Mori H., and Cline K. Oligomers of Tha4 organize at the thylakoid Tat translocase during protein transport. J. Biol. Chem. 281 (2006) 5476-5483
    • (2006) J. Biol. Chem. , vol.281 , pp. 5476-5483
    • Dabney-Smith, C.1    Mori, H.2    Cline, K.3
  • 8
    • 10744228022 scopus 로고    scopus 로고
    • Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
    • Alami M., Luke I., Deitermann S., Eisner G., Koch H.G., Brunner J., and Müller M. Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell 12 (2003) 937-946
    • (2003) Mol. Cell , vol.12 , pp. 937-946
    • Alami, M.1    Luke, I.2    Deitermann, S.3    Eisner, G.4    Koch, H.G.5    Brunner, J.6    Müller, M.7
  • 9
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban M.J. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J. Mol. Biol. 104 (1976) 541-555
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 10
    • 0034595796 scopus 로고    scopus 로고
    • TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in Sec-independent protein export
    • Wexler M., Sargent F., Jack R.L., Stanley N.R., Bogsch E.G., Robinson C., Berks B.C., and Palmer T. TatD is a cytoplasmic protein with DNase activity. No requirement for TatD family proteins in Sec-independent protein export. J. Biol. Chem. 275 (2000) 16717-16722
    • (2000) J. Biol. Chem. , vol.275 , pp. 16717-16722
    • Wexler, M.1    Sargent, F.2    Jack, R.L.3    Stanley, N.R.4    Bogsch, E.G.5    Robinson, C.6    Berks, B.C.7    Palmer, T.8
  • 11
    • 3042589734 scopus 로고    scopus 로고
    • Localization of the Tat translocon components in Escherichia coli
    • Berthelmann F., and Brüser T. Localization of the Tat translocon components in Escherichia coli. FEBS Lett. 569 (2004) 82-88
    • (2004) FEBS Lett. , vol.569 , pp. 82-88
    • Berthelmann, F.1    Brüser, T.2
  • 13
    • 0035917935 scopus 로고    scopus 로고
    • High-cell-density fermentation for production of l-N-carbamoylase using an expression system based on the Escherichia coli rhaBAD promoter
    • Wilms B., Hauck A., Reuss M., Syldatk C., Mattes R., Siemann M., and Altenbuchner J. High-cell-density fermentation for production of l-N-carbamoylase using an expression system based on the Escherichia coli rhaBAD promoter. Biotechnol. Bioeng. 73 (2001) 95-103
    • (2001) Biotechnol. Bioeng. , vol.73 , pp. 95-103
    • Wilms, B.1    Hauck, A.2    Reuss, M.3    Syldatk, C.4    Mattes, R.5    Siemann, M.6    Altenbuchner, J.7
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0039351902 scopus 로고    scopus 로고
    • Evidence against the double-arginine motif as the only determinant for protein translocation by a novel Sec-independent pathway in Escherichia coli
    • Brüser T., Deutzmann R., and Dahl C. Evidence against the double-arginine motif as the only determinant for protein translocation by a novel Sec-independent pathway in Escherichia coli. FEMS Microbiol. Lett. 164 (1998) 329-336
    • (1998) FEMS Microbiol. Lett. , vol.164 , pp. 329-336
    • Brüser, T.1    Deutzmann, R.2    Dahl, C.3
  • 17
    • 14644439237 scopus 로고    scopus 로고
    • Characterisation of Tat protein transport complexes carrying inactivating mutations
    • McDevitt C.A., Hicks M.G., Palmer T., and Berks B.C. Characterisation of Tat protein transport complexes carrying inactivating mutations. Biochem. Biophys. Res. Commun. 329 (2005) 693-698
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , pp. 693-698
    • McDevitt, C.A.1    Hicks, M.G.2    Palmer, T.3    Berks, B.C.4
  • 18
    • 0030577385 scopus 로고    scopus 로고
    • 0 sector is a substrate of the FtsH protease in Escherichia coli
    • 0 sector is a substrate of the FtsH protease in Escherichia coli. FEBS Lett. 399 (1996) 26-28
    • (1996) FEBS Lett. , vol.399 , pp. 26-28
    • Akiyama, Y.1    Kihara, A.2    Ito, K.3
  • 19
    • 0029017127 scopus 로고
    • FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit
    • Kihara A., Akiyama Y., and Ito K. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc. Natl. Acad. Sci. USA 92 (1995) 4532-4536
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4532-4536
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 20
    • 9644273939 scopus 로고    scopus 로고
    • The core TatABC complex of the twin-arginine translocase in Escherichia coli: TatC drives assembly whereas TatA is essential for stability
    • Mangels D., Mathers J., Bolhuis A., and Robinson C. The core TatABC complex of the twin-arginine translocase in Escherichia coli: TatC drives assembly whereas TatA is essential for stability. J. Mol. Biol. 345 (2005) 415-423
    • (2005) J. Mol. Biol. , vol.345 , pp. 415-423
    • Mangels, D.1    Mathers, J.2    Bolhuis, A.3    Robinson, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.