메뉴 건너뛰기




Volumn 579, Issue 5, 2005, Pages 1267-1271

Escherichia coli SecA truncated at its termini is functional and dimeric

Author keywords

ATPase; Dimerization; Protein secretion; SecA; Translocase

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CARRIER PROTEIN; MUTANT PROTEIN; NUCLEOTIDE; PROTEIN SECA;

EID: 13844298669     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.01.025     Document Type: Article
Times cited : (36)

References (27)
  • 1
    • 4444290475 scopus 로고    scopus 로고
    • Structure and function of SecA, the preprotein translocase nanomotor
    • E. Vrontou, and A. Economou Structure and function of SecA, the preprotein translocase nanomotor BBA Mol. Cell Rev. 2004
    • (2004) BBA Mol. Cell Rev.
    • Vrontou, E.1    Economou, A.2
  • 3
    • 0037134449 scopus 로고    scopus 로고
    • Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain
    • C. Baud, S. Karamanou, G. Sianidis, E. Vrontou, A.S. Politou, and A. Economou Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain J. Biol. Chem. 277 2002 13724 13731
    • (2002) J. Biol. Chem. , vol.277 , pp. 13724-13731
    • Baud, C.1    Karamanou, S.2    Sianidis, G.3    Vrontou, E.4    Politou, A.S.5    Economou, A.6
  • 4
    • 0037144467 scopus 로고    scopus 로고
    • Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA
    • J.F. Hunt, S. Weinkauf, L. Henry, J.J. Fak, P. McNicholas, D.B. Oliver, and J. Deisenhofer Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA Science 297 2002 2018 2026
    • (2002) Science , vol.297 , pp. 2018-2026
    • Hunt, J.F.1    Weinkauf, S.2    Henry, L.3    Fak, J.J.4    McNicholas, P.5    Oliver, D.B.6    Deisenhofer, J.7
  • 8
    • 0025959111 scopus 로고
    • SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer
    • M. Akita, A. Shinkai, S. Matsuyama, and S. Mizushima SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer Biochem. Biophys. Res. Commun. 174 1991 211 216
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 211-216
    • Akita, M.1    Shinkai, A.2    Matsuyama, S.3    Mizushima, S.4
  • 9
    • 0030569557 scopus 로고    scopus 로고
    • The carboxyl-terminal region is essential for Sec-A dimerization
    • M. Hirano, S. Matsuyama, and H. Tokuda The carboxyl-terminal region is essential for Sec-A dimerization Biochem. Biophys. Res. Commun. 229 1996 90 95
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 90-95
    • Hirano, M.1    Matsuyama, S.2    Tokuda, H.3
  • 10
  • 11
    • 0027769773 scopus 로고
    • SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer
    • A.J. Driessen SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer Biochemistry 32 1993 13190 13197
    • (1993) Biochemistry , vol.32 , pp. 13190-13197
    • Driessen, A.J.1
  • 12
    • 0037009514 scopus 로고    scopus 로고
    • Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane
    • E. Or, A. Navon, and T. Rapoport Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane EMBO J. 21 2002 4470 4479
    • (2002) EMBO J. , vol.21 , pp. 4470-4479
    • Or, E.1    Navon, A.2    Rapoport, T.3
  • 13
    • 0036303451 scopus 로고    scopus 로고
    • The ATPase domain of SecA can form a tetramer in solution
    • B.R. Dempsey, A. Economou, S.D. Dunn, and B.H. Shilton The ATPase domain of SecA can form a tetramer in solution J. Mol. Biol. 315 2002 831 843
    • (2002) J. Mol. Biol. , vol.315 , pp. 831-843
    • Dempsey, B.R.1    Economou, A.2    Dunn, S.D.3    Shilton, B.H.4
  • 14
    • 2542450771 scopus 로고    scopus 로고
    • Global co-ordination of protein translocation by the SecA IRA1 switch
    • E. Vrontou, S. Karamanou, C. Baud, G. Sianidis, and A. Economou Global co-ordination of protein translocation by the SecA IRA1 switch J. Biol. Chem. 279 2004 22490 22497
    • (2004) J. Biol. Chem. , vol.279 , pp. 22490-22497
    • Vrontou, E.1    Karamanou, S.2    Baud, C.3    Sianidis, G.4    Economou, A.5
  • 15
    • 0042347712 scopus 로고    scopus 로고
    • Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution
    • H. Ding, J.F. Hunt, I. Mukerji, and D. Oliver Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution Biochemistry 42 2003 8729 8738
    • (2003) Biochemistry , vol.42 , pp. 8729-8738
    • Ding, H.1    Hunt, J.F.2    Mukerji, I.3    Oliver, D.4
  • 19
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • R. Lill, W. Dowhan, and W. Wickner The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins Cell 60 1990 271 280
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 20
    • 0034618026 scopus 로고    scopus 로고
    • Dissecting the translocase and integrase functions of the Escherichia coli SecYEG translocon
    • H.G. Koch, and M. Muller Dissecting the translocase and integrase functions of the Escherichia coli SecYEG translocon J. Cell Biol. 150 2000 689 694
    • (2000) J. Cell Biol. , vol.150 , pp. 689-694
    • Koch, H.G.1    Muller, M.2
  • 21
    • 0027488666 scopus 로고
    • Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase
    • C. Mitchell, and D. Oliver Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase Mol. Microbiol. 10 1993 483 497
    • (1993) Mol. Microbiol. , vol.10 , pp. 483-497
    • Mitchell, C.1    Oliver, D.2
  • 22
    • 0034602846 scopus 로고    scopus 로고
    • Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor
    • K. Beck, L.F. Wu, J. Brunner, and M. Muller Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor EMBO J. 19 2000 134 143
    • (2000) EMBO J. , vol.19 , pp. 134-143
    • Beck, K.1    Wu, L.F.2    Brunner, J.3    Muller, M.4
  • 23
    • 4444316122 scopus 로고    scopus 로고
    • Helicase Motif III in SecA is essential for coupling preprotein binding to translocation ATPase
    • E. Papanikou, S. Karamanou, C. Baud, G. Sianidis, M. Frank, and A. Economou Helicase Motif III in SecA is essential for coupling preprotein binding to translocation ATPase EMBO Rep. 5 2004 807 811
    • (2004) EMBO Rep. , vol.5 , pp. 807-811
    • Papanikou, E.1    Karamanou, S.2    Baud, C.3    Sianidis, G.4    Frank, M.5    Economou, A.6
  • 25
    • 0025310526 scopus 로고
    • Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region
    • S. Matsuyama, E. Kimura, and S. Mizushima Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region J. Biol. Chem. 265 1990 8760 8765
    • (1990) J. Biol. Chem. , vol.265 , pp. 8760-8765
    • Matsuyama, S.1    Kimura, E.2    Mizushima, S.3
  • 27
    • 0031820398 scopus 로고    scopus 로고
    • Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles
    • H. Mori, H. Sugiyama, M. Yamanaka, K. Sato, M. Tagaya, and S. Mizushima Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles J. Biochem. (Tokyo) 124 1998 122 129
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 122-129
    • Mori, H.1    Sugiyama, H.2    Yamanaka, M.3    Sato, K.4    Tagaya, M.5    Mizushima, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.