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Volumn 190, Issue 4, 2008, Pages 1413-1418

Additional in vitro and in vivo evidence for SecA functioning as dimers in the membrane: Dissociation into monomers is not essential for protein translocation in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DIMER; MONOMER; PROTEIN SECA; SECRETORY PROTEIN;

EID: 38949141646     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01633-07     Document Type: Article
Times cited : (33)

References (33)
  • 1
    • 0025959111 scopus 로고
    • SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer
    • Akita, M., A. Shinkai, S. Matsuyama, and S. Mizushima. 1991. SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer. Biochem. Biophys. Res. Commun. 174:211-216.
    • (1991) Biochem. Biophys. Res. Commun , vol.174 , pp. 211-216
    • Akita, M.1    Shinkai, A.2    Matsuyama, S.3    Mizushima, S.4
  • 2
    • 34247214427 scopus 로고    scopus 로고
    • Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
    • Alami, M., K. Dalal, B. Lelj-Garolla, S. G. Sligar, and F. Duong. 2007. Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA. EMBO J. 26:1995-2004.
    • (2007) EMBO J , vol.26 , pp. 1995-2004
    • Alami, M.1    Dalal, K.2    Lelj-Garolla, B.3    Sligar, S.G.4    Duong, F.5
  • 4
    • 0024291341 scopus 로고
    • SecA protein is required for secretory protein translocation into Escherichia coli membrane-vesicles
    • Cabelli, R. J., L. L. Chen, P. C. Tai, and D. B. Oliver. 1988. SecA protein is required for secretory protein translocation into Escherichia coli membrane-vesicles. Cell 55:683-692.
    • (1988) Cell , vol.55 , pp. 683-692
    • Cabelli, R.J.1    Chen, L.L.2    Tai, P.C.3    Oliver, D.B.4
  • 5
    • 0021909844 scopus 로고
    • Alkaline phosphatase and OmpA protein can be translocated posttranslationally into membrane vesicles of Escherichia coli
    • Chen, L., D. Rhoads, and P. C. Tai. 1985. Alkaline phosphatase and OmpA protein can be translocated posttranslationally into membrane vesicles of Escherichia coli. J. Bacteriol. 161:973-980.
    • (1985) J. Bacteriol , vol.161 , pp. 973-980
    • Chen, L.1    Rhoads, D.2    Tai, P.C.3
  • 6
    • 27444439568 scopus 로고    scopus 로고
    • de Keyzer, J., E. O. van der Sluis, R. E. Spelbrink, N. Nijstad, B. de Kruijff, N. Nouwen, C. van der Does, and A. J. Driessen. 2005. Covalently dimerized SecA is functional in protein translocation. J. Biol. Chem. 280:35255-35260.
    • de Keyzer, J., E. O. van der Sluis, R. E. Spelbrink, N. Nijstad, B. de Kruijff, N. Nouwen, C. van der Does, and A. J. Driessen. 2005. Covalently dimerized SecA is functional in protein translocation. J. Biol. Chem. 280:35255-35260.
  • 7
    • 0042347712 scopus 로고    scopus 로고
    • Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution
    • Ding, H., J. F. Hunt, I. Mukerji, and D. Oliver. 2003. Bacillus subtilis SecA ATPase exists as an antiparallel dimer in solution. Biochemistry 42:8729-8738.
    • (2003) Biochemistry , vol.42 , pp. 8729-8738
    • Ding, H.1    Hunt, J.F.2    Mukerji, I.3    Oliver, D.4
  • 8
    • 0027769773 scopus 로고
    • SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer
    • Driessen, A. J. 1993. SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer. Biochemistry 32: 13190-13197.
    • (1993) Biochemistry , vol.32 , pp. 13190-13197
    • Driessen, A.J.1
  • 9
    • 0022532398 scopus 로고
    • Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles
    • Geller, B. L., N. R. Mowa, and W. Wickner. 1986. Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles. Proc. Natl. Acad. Sci. USA 83:4219-4222.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4219-4222
    • Geller, B.L.1    Mowa, N.R.2    Wickner, W.3
  • 10
    • 34547123821 scopus 로고    scopus 로고
    • Allosteric regulation of SecA: Magnesium-mediated control of conformation and activity
    • Gold, V. A., A. Robson, A. R. Clarke, and I. Collinson. 2007. Allosteric regulation of SecA: magnesium-mediated control of conformation and activity. J. Biol. Chem. 282:17424-17432.
    • (2007) J. Biol. Chem , vol.282 , pp. 17424-17432
    • Gold, V.A.1    Robson, A.2    Clarke, A.R.3    Collinson, I.4
  • 11
    • 0030569557 scopus 로고    scopus 로고
    • The carboxyl-terminal region is essential for Sec-A dimerization
    • Hirano, M., S. Matsuyama, and H. Tokuda. 1996. The carboxyl-terminal region is essential for Sec-A dimerization. Biochem. Biophys. Res. Commun. 229:90-95.
    • (1996) Biochem. Biophys. Res. Commun , vol.229 , pp. 90-95
    • Hirano, M.1    Matsuyama, S.2    Tokuda, H.3
  • 12
    • 0037144467 scopus 로고    scopus 로고
    • Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA
    • Hunt, J. F., S. Weinkauf, L. Henry, J. J. Fak, P. McNicholas, D. B. Oliver, and J. Deisenhofer. 2002. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Science 297:2018-2026.
    • (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
  • 13
    • 33644904085 scopus 로고    scopus 로고
    • SecA dimer cross-linked at its subunit interface is functional for protein translocation
    • Jilaveanu, L. B., and D. Oliver. 2006. SecA dimer cross-linked at its subunit interface is functional for protein translocation. J. Bacteriol. 188:335-338.
    • (2006) J. Bacteriol , vol.188 , pp. 335-338
    • Jilaveanu, L.B.1    Oliver, D.2
  • 14
  • 16
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • Lill, R., W. Dowhan, and W. Wickner. 1990. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins. Cell 60:271-280.
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 17
    • 0030930246 scopus 로고    scopus 로고
    • Manting, E. H., C. van der Does, and A. J. Driessen. 1997. In vivo cross-linking of the SecA and SecY subunits of the Escherichia coli preprotein translocase. J. Bacteriol. 179:5699-5704.
    • Manting, E. H., C. van der Does, and A. J. Driessen. 1997. In vivo cross-linking of the SecA and SecY subunits of the Escherichia coli preprotein translocase. J. Bacteriol. 179:5699-5704.
  • 18
    • 0027488666 scopus 로고
    • Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase
    • Mitchell, C., and D. Oliver. 1993. Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase. Mol. Microbiol. 10:483-497.
    • (1993) Mol. Microbiol , vol.10 , pp. 483-497
    • Mitchell, C.1    Oliver, D.2
  • 19
    • 0034721917 scopus 로고    scopus 로고
    • Two independent mechanisms down-regulate the intrinsic SecA ATPase activity
    • Nakatogawa, H., H. Mori, and K. Ito. 2000. Two independent mechanisms down-regulate the intrinsic SecA ATPase activity. J. Biol. Chem. 275:33209-33212.
    • (2000) J. Biol. Chem , vol.275 , pp. 33209-33212
    • Nakatogawa, H.1    Mori, H.2    Ito, K.3
  • 20
    • 0027455603 scopus 로고
    • SecA protein: Autoregulated ATPase catalysing preprotein insertion and translocation across the Escherichia coli inner membrane
    • Oliver, D. B. 1993. SecA protein: autoregulated ATPase catalysing preprotein insertion and translocation across the Escherichia coli inner membrane. Mol. Microbiol. 7:159-165.
    • (1993) Mol. Microbiol , vol.7 , pp. 159-165
    • Oliver, D.B.1
  • 21
    • 0019413905 scopus 로고    scopus 로고
    • Oliver, D. B., and J. Beckwith. 1981. E. coli mutant pleiotropically defective in the export of secreted proteins. Cell 25:765-772.
    • Oliver, D. B., and J. Beckwith. 1981. E. coli mutant pleiotropically defective in the export of secreted proteins. Cell 25:765-772.
  • 22
    • 15744404686 scopus 로고    scopus 로고
    • The bacterial ATPase SecA functions as a monomer in protein translocation
    • Or, E., D. Boyd, S. Gon, J. Beckwith, and T. Rapoport. 2005. The bacterial ATPase SecA functions as a monomer in protein translocation. J. Biol. Chem. 280:9097-9105.
    • (2005) J. Biol. Chem , vol.280 , pp. 9097-9105
    • Or, E.1    Boyd, D.2    Gon, S.3    Beckwith, J.4    Rapoport, T.5
  • 23
    • 0037009514 scopus 로고    scopus 로고
    • Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane
    • Or, E., A. Navon, and T. Rapoport. 2002. Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane. EMBO J. 21:4470-4479.
    • (2002) EMBO J , vol.21 , pp. 4470-4479
    • Or, E.1    Navon, A.2    Rapoport, T.3
  • 24
    • 34249698314 scopus 로고    scopus 로고
    • Cross-linked SecA dimers are not functional in protein translocation
    • Or, E., and T. Rapoport. 2007. Cross-linked SecA dimers are not functional in protein translocation. FEBS Lett. 581:2616-2620.
    • (2007) FEBS Lett , vol.581 , pp. 2616-2620
    • Or, E.1    Rapoport, T.2
  • 26
    • 0037767478 scopus 로고    scopus 로고
    • Molecular and functional analysis of the lepB gene, encoding a type I signal peptidase from Rickettsia rickettsii and Rickettsia typhi
    • Rahman, M. S., J. A. Simser, K. R. Macaluso, and A. F. Azad. 2003. Molecular and functional analysis of the lepB gene, encoding a type I signal peptidase from Rickettsia rickettsii and Rickettsia typhi. J. Bacteriol. 185: 4578-4584.
    • (2003) J. Bacteriol , vol.185 , pp. 4578-4584
    • Rahman, M.S.1    Simser, J.A.2    Macaluso, K.R.3    Azad, A.F.4
  • 27
    • 16244410498 scopus 로고    scopus 로고
    • Asymmetric binding between SecA and SecB two symmetric proteins: Implications for function in export
    • Randall, L. L., J. M. Crane, A. A. Lilly, G. Liu, C. Mao, C. N. Patel, and S. J. Hardy. 2005. Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export. J. Mol. Biol. 348:479-489.
    • (2005) J. Mol. Biol , vol.348 , pp. 479-489
    • Randall, L.L.1    Crane, J.M.2    Lilly, A.A.3    Liu, G.4    Mao, C.5    Patel, C.N.6    Hardy, S.J.7
  • 28
    • 0023678449 scopus 로고
    • Nucleotide-sequence of the secA gene and secA (Ts) mutations preventing protein export in Escherichia coli
    • Schmidt, M. G., E. E. Rollo, J. Grodberg, and D. B. Oliver. 1988. Nucleotide-sequence of the secA gene and secA (Ts) mutations preventing protein export in Escherichia coli. J. Bacteriol. 170:3404-3414.
    • (1988) J. Bacteriol , vol.170 , pp. 3404-3414
    • Schmidt, M.G.1    Rollo, E.E.2    Grodberg, J.3    Oliver, D.B.4
  • 29
    • 33744954168 scopus 로고    scopus 로고
    • Effects of signal peptide and adenylate on the oligomerization and membrane binding of soluble SecA
    • Shin, J. Y., M. Kim, and T. Ahn. 2006. Effects of signal peptide and adenylate on the oligomerization and membrane binding of soluble SecA. J. Biochem. Mol. Biol. 39:319-328.
    • (2006) J. Biochem. Mol. Biol , vol.39 , pp. 319-328
    • Shin, J.Y.1    Kim, M.2    Ahn, T.3
  • 30
    • 2342463112 scopus 로고
    • Streptomycin causes misreading of natural messenger by interacting with ribosomes after initiation
    • Tai, P. C., B. J. Wallace, and B. D. Davis. 1978. Streptomycin causes misreading of natural messenger by interacting with ribosomes after initiation. Proc. Natl. Acad. Sci. USA 75:275-279.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 275-279
    • Tai, P.C.1    Wallace, B.J.2    Davis, B.D.3
  • 31
    • 0037389586 scopus 로고    scopus 로고
    • Ring-like pore structures of SecA: Implication for bacterial protein-conducting channels
    • Wang, H. W., Y. Chen, H. Yang, X. Chen, M. X. Duan, P. C. Tai, and S. F. Sui. 2003. Ring-like pore structures of SecA: implication for bacterial protein-conducting channels. Proc. Natl. Acad. Sci. USA 100:4221-4226.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4221-4226
    • Wang, H.W.1    Chen, Y.2    Yang, H.3    Chen, X.4    Duan, M.X.5    Tai, P.C.6    Sui, S.F.7
  • 32
    • 0036129188 scopus 로고    scopus 로고
    • Complex behavior in solution of homodimeric SecA
    • Woodbury, R. L., S. J. Hardy, and L. L. Randall. 2002. Complex behavior in solution of homodimeric SecA. Protein Sci. 11:875-882.
    • (2002) Protein Sci , vol.11 , pp. 875-882
    • Woodbury, R.L.1    Hardy, S.J.2    Randall, L.L.3
  • 33
    • 0345832155 scopus 로고    scopus 로고
    • Cys32 and His105 are the critical residues for the calcium-dependent cysteine proteolytic activity of CvaB, an ATP-binding cassette transporter
    • Wu, K. H., and P. C. Tai. 2004. Cys32 and His105 are the critical residues for the calcium-dependent cysteine proteolytic activity of CvaB, an ATP-binding cassette transporter. J. Biol. Chem. 279:901-909.
    • (2004) J. Biol. Chem , vol.279 , pp. 901-909
    • Wu, K.H.1    Tai, P.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.