메뉴 건너뛰기




Volumn 191, Issue 3, 2009, Pages 978-984

Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GALAPTIN; OUTER MEMBRANE PROTEIN A; PERIPLASMIC PROTEIN; POLYPEPTIDE; PROTEIN SECA; PROTEIN SECB; ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; CARRIER PROTEIN; PEPTIDE; SECA PROTEIN, BACTERIA; SECB PROTEIN, BACTERIA;

EID: 63449140188     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01321-08     Document Type: Article
Times cited : (24)

References (34)
  • 1
    • 0035942238 scopus 로고    scopus 로고
    • Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: Use of a photoactivatable reagent
    • Cai, K., Y. Itoh, and H. G. Khorana. 2001. Mapping of contact sites in complex formation between transducin and light-activated rhodopsin by covalent crosslinking: use of a photoactivatable reagent. Proc. Natl. Acad. Sci. USA 98:4877-4882.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4877-4882
    • Cai, K.1    Itoh, Y.2    Khorana, H.G.3
  • 2
    • 57649143096 scopus 로고    scopus 로고
    • Full-length Escherichia coli SecA dimerizes in a closed conformation in solution as determined by cryo-electron microscopy
    • Chen, Y., X. Pan, Y. Tang, S. Quan, P. C. Tai, and S.-F. Sui. 2008. Full-length Escherichia coli SecA dimerizes in a closed conformation in solution as determined by cryo-electron microscopy. J. Biol. Chem. 283:28783-28787.
    • (2008) J. Biol. Chem , vol.283 , pp. 28783-28787
    • Chen, Y.1    Pan, X.2    Tang, Y.3    Quan, S.4    Tai, P.C.5    Sui, S.-F.6
  • 3
    • 49349084439 scopus 로고    scopus 로고
    • SecA. the motor of the secretion machine, binds diverse partners on one interactive surface
    • Cooper, D. B., V. F. Smith, J. M. Crane, H. C. Roth, A. A. Lilly, and L. L. Randall. 2008. SecA. the motor of the secretion machine, binds diverse partners on one interactive surface. J. Mol. Biol. 382:74-87.
    • (2008) J. Mol. Biol , vol.382 , pp. 74-87
    • Cooper, D.B.1    Smith, V.F.2    Crane, J.M.3    Roth, H.C.4    Lilly, A.A.5    Randall, L.L.6
  • 4
    • 25144470549 scopus 로고    scopus 로고
    • Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: Insight into the mechanism of ligand transfer during protein export
    • Crane, J. M., C. Mao, A. A. Lilly, V. F. Smith, Y. Suo, W. L. Hubbell, and L. L. Randall. 2005. Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export. J. Mol. Biol. 353:295-307.
    • (2005) J. Mol. Biol , vol.353 , pp. 295-307
    • Crane, J.M.1    Mao, C.2    Lilly, A.A.3    Smith, V.F.4    Suo, Y.5    Hubbell, W.L.6    Randall, L.L.7
  • 5
    • 55749113726 scopus 로고    scopus 로고
    • Re-examination of the role of the amino terminus of SecA in promoting its dimerization and functional state
    • Das, S., E. Stivison, E. Folta-Stogniew, and D. Oliver. 2008. Re-examination of the role of the amino terminus of SecA in promoting its dimerization and functional state. J. Bacteriol. 190:7302-7307.
    • (2008) J. Bacteriol , vol.190 , pp. 7302-7307
    • Das, S.1    Stivison, E.2    Folta-Stogniew, E.3    Oliver, D.4
  • 6
    • 0344983315 scopus 로고    scopus 로고
    • Dekker, C., B. de Kruijff, and P. Gros. 2003. Crystal structure of SecB from Escherichia coli. J. Struct. Biol. 144:313-319.
    • Dekker, C., B. de Kruijff, and P. Gros. 2003. Crystal structure of SecB from Escherichia coli. J. Struct. Biol. 144:313-319.
  • 7
    • 0041736710 scopus 로고    scopus 로고
    • Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
    • Duong, F. 2003. Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase. EMBO J. 22:4375-4384.
    • (2003) EMBO J , vol.22 , pp. 4375-4384
    • Duong, F.1
  • 8
    • 2942588637 scopus 로고    scopus 로고
    • Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state
    • Fak, J. J., A. Itkin, D. D. Ciobanu, E. C. Lin, X. J. Song, Y. T. Chou, L. M. Gierasch, and J. F. Hunt. 2004. Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state. Biochemistry 43:7307-7327.
    • (2004) Biochemistry , vol.43 , pp. 7307-7327
    • Fak, J.J.1    Itkin, A.2    Ciobanu, D.D.3    Lin, E.C.4    Song, X.J.5    Chou, Y.T.6    Gierasch, L.M.7    Hunt, J.F.8
  • 10
    • 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
  • 11
    • 0029128122 scopus 로고
    • Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB
    • Kimsey, H. H., M. D. Dagarag, and C. A. Kumamoto. 1995. Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB. J. Biol. Chem. 270:22831-22835.
    • (1995) J. Biol. Chem , vol.270 , pp. 22831-22835
    • Kimsey, H.H.1    Dagarag, M.D.2    Kumamoto, C.A.3
  • 12
    • 0021867206 scopus 로고
    • Evidence for specificity at an early step in protein export in Escherichia coli
    • Kumamoto, C. A., and J. Beckwith. 1985. Evidence for specificity at an early step in protein export in Escherichia coli. J. Bacteriol. 163:267-274.
    • (1985) J. Bacteriol , vol.163 , pp. 267-274
    • Kumamoto, C.A.1    Beckwith, J.2
  • 13
    • 0037184003 scopus 로고    scopus 로고
    • Organization of the receptor-kinase signaling array that regulates Escherichia coli Chemotaxis
    • Levit, M. N., T. W. Grebe, and J. B. Stock. 2002. Organization of the receptor-kinase signaling array that regulates Escherichia coli Chemotaxis. J. Biol. Chem. 277:36748-36754.
    • (2002) J. Biol. Chem , vol.277 , pp. 36748-36754
    • Levit, M.N.1    Grebe, T.W.2    Stock, J.B.3
  • 14
    • 0024461425 scopus 로고
    • SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli
    • LUI, R., K. Cunningham, L. A. Brundage, K. Ito, D, Oliver, and W. Wickner. 1989. SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli. EMBO J. 8:961-966.
    • (1989) EMBO J , vol.8 , pp. 961-966
    • Cunningham, L.R.K.1    Brundage, L.A.2    Ito, K.3    Oliver, D.4    Wickner, W.5
  • 15
    • 0025039566 scopus 로고
    • SecE-dependent overproduction of SecY in Escherichia coli. Evidence for interaction between two components of the secretory machinery
    • Matsuyama, S., J. Akimaru, and S. Mizushima. 1990. SecE-dependent overproduction of SecY in Escherichia coli. Evidence for interaction between two components of the secretory machinery. FEBS Lett. 269:96-100.
    • (1990) FEBS Lett , vol.269 , pp. 96-100
    • Matsuyama, S.1    Akimaru, J.2    Mizushima, S.3
  • 16
    • 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
    • Mori, H., H. Sugiyama, M. Yamanaka, K. Sato, M. Tagaya, and S. Mizushima, 1998. Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. J. Biochem. 124:122-129.
    • (1998) J. Biochem , vol.124 , pp. 122-129
    • Mori, H.1    Sugiyama, H.2    Yamanaka, M.3    Sato, K.4    Tagaya, M.5    Mizushima, S.6
  • 17
  • 18
    • 33947717366 scopus 로고    scopus 로고
    • Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel
    • Osborne, A. R., and T. A. Rapoport. 2007. Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel. Cell 129:97-110.
    • (2007) Cell , vol.129 , pp. 97-110
    • Osborne, A.R.1    Rapoport, T.A.2
  • 20
    • 35348908966 scopus 로고    scopus 로고
    • Bacterial protein secretion through the translocase nanomachine
    • Papanikou, E., S. Karamanou, and A. Economou. 2007. Bacterial protein secretion through the translocase nanomachine. Nat. Rev. Microbiol. 5:839-851.
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 839-851
    • Papanikou, E.1    Karamanou, S.2    Economou, A.3
  • 21
    • 33744454411 scopus 로고    scopus 로고
    • Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export
    • Patel, C. N., V. F. Smith, and L. L. Randall. 2006. Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export. Protein Sci. 15:1379-1386.
    • (2006) Protein Sci , vol.15 , pp. 1379-1386
    • Patel, C.N.1    Smith, V.F.2    Randall, L.L.3
  • 22
    • 0030752693 scopus 로고    scopus 로고
    • Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding
    • Ramamurthy, V., and D. Oliver. 1997. Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding. J. Biol. Chem. 272:23239-23246.
    • (1997) J. Biol. Chem , vol.272 , pp. 23239-23246
    • Ramamurthy, V.1    Oliver, D.2
  • 23
    • 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. S. 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.S.7
  • 24
    • 1842559293 scopus 로고    scopus 로고
    • Sites of interaction between SecA and the chaperone SecB, two proteins involved in export
    • Randall, L. L., J. M. Crane, G. Liu, and S. J. S. Hardy. 2004. Sites of interaction between SecA and the chaperone SecB, two proteins involved in export. Protein Sci. 13:1124-1133.
    • (2004) Protein Sci , vol.13 , pp. 1124-1133
    • Randall, L.L.1    Crane, J.M.2    Liu, G.3    Hardy, S.J.S.4
  • 25
    • 0026073817 scopus 로고
    • H and ATP function at different steps of the catalytic evele of preprotein translocase
    • H and ATP function at different steps of the catalytic evele of preprotein translocase. Cell 64:927-939.
    • (1991) Cell , vol.64 , pp. 927-939
    • Schiebel, E.1    Driessen, A.J.2    Hartl, F.U.3    Wickner, W.4
  • 28
    • 0030798169 scopus 로고    scopus 로고
    • Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands
    • Topping, T. B., and L. L. Randall. 1997. Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands. J. Biol. Chem. 272:19314-19318.
    • (1997) J. Biol. Chem , vol.272 , pp. 19314-19318
    • Topping, T.B.1    Randall, L.L.2
  • 30
    • 33750846046 scopus 로고    scopus 로고
    • Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer
    • Vassylyev, D. G., H. Mori, M. N. Vassylyeva, T. Tsukazaki, Y, Kimura, T. H. Tahirov, and K. Ito. 2006. Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer. J. Mol. Biol. 364:248-258.
    • (2006) J. Mol. Biol , vol.364 , pp. 248-258
    • Vassylyev, D.G.1    Mori, H.2    Vassylyeva, M.N.3    Tsukazaki, T.4    Kimura, Y.5    Tahirov, T.H.6    Ito, K.7
  • 31
    • 0036129188 scopus 로고    scopus 로고
    • Complex behavior in solution of homodimeric SecA
    • Woodbury, R. L., S. J. S. 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.S.2    Randall, L.L.3
  • 32
    • 0034604633 scopus 로고    scopus 로고
    • Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions
    • Woodbury, R. L., T. B. Topping, D. L. Diamond, D. Suciu, C. A. Kumamoto, S. J. S. Hardy, and L. L. Randall. 2000. Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions. J. Biol. Chem. 275:24191- 24198.
    • (2000) J. Biol. Chem , vol.275 , pp. 24191-24198
    • Woodbury, R.L.1    Topping, T.B.2    Diamond, D.L.3    Suciu, D.4    Kumamoto, C.A.5    Hardy, S.J.S.6    Randall, L.L.7
  • 33
    • 0033675260 scopus 로고    scopus 로고
    • Crystal structure of the bacterial protein export chaperone SecB
    • Xu, Z., J. D. Knafels, and K. Yoshino. 2000. Crystal structure of the bacterial protein export chaperone SecB. Nat. Struct. Biol. 7:1172-1177.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 1172-1177
    • Xu, Z.1    Knafels, J.D.2    Yoshino, K.3
  • 34
    • 33750821188 scopus 로고    scopus 로고
    • A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA
    • Zimmer, J., W. Li, and T. A. Rapoport 2006. A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA. J. Mol. Biol. 364:259-265.
    • (2006) J. Mol. Biol , vol.364 , pp. 259-265
    • Zimmer, J.1    Li, W.2    Rapoport, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.