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Volumn 10, Issue 10, 2002, Pages 1415-1424

Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8

Author keywords

AAA ATPase; FtsH; Hexameric ring structure; Metalloprotease; Substrate translocation

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATASE; METALLOPROTEINASE; METALLOPROTEINASE FTSH; UNCLASSIFIED DRUG;

EID: 0036773132     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00855-9     Document Type: Article
Times cited : (94)

References (52)
  • 1
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman S. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30:1996;465-506.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 2
    • 0027535381 scopus 로고
    • The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression
    • Tomoyasu T., Yuki T., Morimura S., Mori H., Yamanaka K., Niki H., Hiraga S., Ogura T. The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression. J. Bacteriol. 175:1993;1344-1351.
    • (1993) J. Bacteriol. , vol.175 , pp. 1344-1351
    • Tomoyasu, T.1    Yuki, T.2    Morimura, S.3    Mori, H.4    Yamanaka, K.5    Niki, H.6    Hiraga, S.7    Ogura, T.8
  • 5
    • 0028985616 scopus 로고
    • Degradation of σ 32, the heat shock regulator in Escherichia coli, is governed by HflB
    • Herman C., Thevenet D., D'Ari R., Bouloc P. Degradation of σ 32, the heat shock regulator in Escherichia coli, is governed by HflB. Proc. Natl. Acad. Sci. USA. 92:1995;3516-3520.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3516-3520
    • Herman, C.1    Thevenet, D.2    D'Ari, R.3    Bouloc, P.4
  • 7
    • 0029989855 scopus 로고    scopus 로고
    • FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins
    • Akiyama Y., Kihara A., Tokuda H., Ito K. FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins. J. Biol. Chem. 271:1996;31196-31201.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31196-31201
    • Akiyama, Y.1    Kihara, A.2    Tokuda, H.3    Ito, K.4
  • 8
    • 0029017127 scopus 로고
    • FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit
    • Kihara A., Akiyama Y., 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
  • 9
    • 0030577385 scopus 로고    scopus 로고
    • Subunit a of proton ATPase Fo sector is a substrate of the FtsH protease in Escherichia coli
    • Akiyama Y., Kihara A., Ito K. Subunit a of proton ATPase Fo 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
  • 10
    • 0032577263 scopus 로고    scopus 로고
    • Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: An implication from the interference by a mutant form of a new substrate protein, YccA
    • Kihara A., Akiyama Y., Ito K. Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex. An implication from the interference by a mutant form of a new substrate protein, YccA J. Mol. Biol. 279:1998;175-188.
    • (1998) J. Mol. Biol. , vol.279 , pp. 175-188
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 11
    • 0033153237 scopus 로고    scopus 로고
    • Dislocation of membrane proteins in FtsH-mediated proteolysis
    • Kihara A., Akiyama Y., Ito K. Dislocation of membrane proteins in FtsH-mediated proteolysis. EMBO J. 18:1999;2970-2981.
    • (1999) EMBO J. , vol.18 , pp. 2970-2981
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 12
    • 0033602381 scopus 로고    scopus 로고
    • Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease
    • Leonhard K., Stiegler A., Neupert W., Langer T. Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease. Nature. 398:1999;348-351.
    • (1999) Nature , vol.398 , pp. 348-351
    • Leonhard, K.1    Stiegler, A.2    Neupert, W.3    Langer, T.4
  • 14
    • 0030867609 scopus 로고    scopus 로고
    • Sequence analysis of the AAA protein family
    • Beyer A. Sequence analysis of the AAA protein family. Protein Sci. 6:1997;2043-2058.
    • (1997) Protein Sci. , vol.6 , pp. 2043-2058
    • Beyer, A.1
  • 15
    • 0032969563 scopus 로고    scopus 로고
    • Aaa+: A class of chaperone-like atpases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald A.F., Aravind L., Spouge J.L., Koonin E.V. Aaa+. a class of chaperone-like atpases associated with the assembly, operation, and disassembly of protein complexes Genome Res. 9:1999;27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 16
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura T., Wilkinson A.J. AAA+ superfamily ATPases. common structure-diverse function Genes Cells. 6:2001;575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 17
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATPases with diverse functions
    • Patel S., Latterich M. The AAA team. related ATPases with diverse functions Trends Cell Biol. 8:1998;65-71.
    • (1998) Trends Cell Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 18
  • 19
    • 0034079766 scopus 로고    scopus 로고
    • FtsH recognizes proteins with unfolded structure and hydrolyzes the carboxyl side of hydrophobic residues
    • Asahara Y., Atsuta K., Motohashi K., Taguchi H., Yohda M., Yoshida M. FtsH recognizes proteins with unfolded structure and hydrolyzes the carboxyl side of hydrophobic residues. J. Biochem. (Tokyo). 127:2000;931-937.
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 931-937
    • Asahara, Y.1    Atsuta, K.2    Motohashi, K.3    Taguchi, H.4    Yohda, M.5    Yoshida, M.6
  • 21
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:1993;123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 24
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell. 94:1998;525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 26
    • 0028840312 scopus 로고
    • FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli
    • Akiyama Y., Yoshihisa T., Ito K. FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 270:1995;23485-23490.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23485-23490
    • Akiyama, Y.1    Yoshihisa, T.2    Ito, K.3
  • 27
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • Sawaya M.R., Guo S., Tabor S., Richardson C.C., Ellenberger T. Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell. 99:1999;167-177.
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 28
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton M.R., Sawaya M.R., Ellenberger T., Wigley D.B. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell. 101:2000;589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 29
    • 1842370904 scopus 로고    scopus 로고
    • Turning off the Ras switch with the flick of a finger
    • Noel J.P. Turning off the Ras switch with the flick of a finger. Nat. Struct. Biol. 4:1997;677-680.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 677-680
    • Noel, J.P.1
  • 31
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH
    • Karata K., Inagawa T., Wilkinson A.J., Tatsuta T., Ogura T. Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. J. Biol. Chem. 274:1999;26225-26232.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26225-26232
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 32
    • 0035116848 scopus 로고    scopus 로고
    • Probing the mechanism of ATP hydrolysis and substrate translocation in the AAA protease FtsH by modeling and mutagenesis
    • Karata K., Verma C.S., Wilkinson A.J., Ogura T. Probing the mechanism of ATP hydrolysis and substrate translocation in the AAA protease FtsH by modeling and mutagenesis. Mol. Microbiol. 39:2001;890-903.
    • (2001) Mol. Microbiol. , vol.39 , pp. 890-903
    • Karata, K.1    Verma, C.S.2    Wilkinson, A.J.3    Ogura, T.4
  • 34
    • 0031803530 scopus 로고    scopus 로고
    • Polypeptide binding of Escherichia coli FtsH (HflB)
    • Akiyama Y., Ehrmann M., Kihara A., Ito K. Polypeptide binding of Escherichia coli FtsH (HflB). Mol. Microbiol. 28:1998;803-812.
    • (1998) Mol. Microbiol. , vol.28 , pp. 803-812
    • Akiyama, Y.1    Ehrmann, M.2    Kihara, A.3    Ito, K.4
  • 36
    • 0033535955 scopus 로고    scopus 로고
    • Lon and Clp family proteases and chaperones share homologous substrate-recognition domains
    • Smith C.K., Baker T.A., Sauer R.T. Lon and Clp family proteases and chaperones share homologous substrate-recognition domains. Proc. Natl. Acad. Sci. USA. 96:1999;6678-6682.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6678-6682
    • Smith, C.K.1    Baker, T.A.2    Sauer, R.T.3
  • 37
    • 0034502532 scopus 로고    scopus 로고
    • Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP
    • Ortega J., Singh S.K., Ishikawa T., Maurizi M.R., Steven A.C. Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol. Cell. 6:2000;1515-1521.
    • (2000) Mol. Cell , vol.6 , pp. 1515-1521
    • Ortega, J.1    Singh, S.K.2    Ishikawa, T.3    Maurizi, M.R.4    Steven, A.C.5
  • 38
    • 0035957317 scopus 로고    scopus 로고
    • ClpA mediates directional translocation of substrate proteins into the ClpP protease
    • Reid B.G., Fenton W.A., Horwich A.L., Weber-Ban E.U. ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proc. Natl. Acad. Sci. USA. 98:2001;3768-3772.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3768-3772
    • Reid, B.G.1    Fenton, W.A.2    Horwich, A.L.3    Weber-Ban, E.U.4
  • 41
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner S., Maurizi M.R., Gottesman S. Posttranslational quality control. folding, refolding, and degrading proteins Science. 286:1999;1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 42
    • 0036077404 scopus 로고    scopus 로고
    • Crystallization of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli
    • Krzywda S., Brzozowski A.M., Karata K., Ogura T., Wilkinson A.J. Crystallization of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli. Acta Crystallogr. D. 58:2002;1066-1067.
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1066-1067
    • Krzywda, S.1    Brzozowski, A.M.2    Karata, K.3    Ogura, T.4    Wilkinson, A.J.5
  • 43
    • 0002414103 scopus 로고
    • Macromolecular data processing
    • V.D. Moras, A.D. Podjarny, & J.C. Thierry. Oxford: Oxford University Press 27-38.pp
    • Leslie A. Macromolecular data processing. Moras V.D., Podjarny A.D., Thierry J.C. Crystal Computing. 1991;Oxford University Press, Oxford. 27-38.pp.
    • (1991) Crystal Computing
    • Leslie, A.1
  • 44
    • 0028103275 scopus 로고
    • Collaborative Computational Project 4) The CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collection in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collection in oscillation mode. Methods Enzymol. 276:1997;307-325.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-325
    • Otwinowski, Z.1    Minor, W.2
  • 48
    • 0033081529 scopus 로고    scopus 로고
    • Rapid automated molecular replacement by evolutionary search
    • Kissinger C.R., Gehlhaar D.K., Fogel D.B. Rapid automated molecular replacement by evolutionary search Acta Crystallogr. D. 55:1999;484-491
    • (1999) Acta Crystallogr. D , vol.55 , pp. 484-491
    • Kissinger, C.R.1    Gehlhaar, D.K.2    Fogel, D.B.3
  • 49
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structure
    • Kraulis P.J. Molscript. a program to produce both detailed and schematic plots of protein structure J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 50
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D-photorealistic molecular graphics
    • Merrit E.A., Bacon D.J. Raster3D-photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 51
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D. 55:1999;938-940.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 52
    • 84986486656 scopus 로고
    • A rapid finite-difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls A., Honig B.J. A rapid finite-difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation. J. Comput. Chem. 12:1991;435-445.
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.J.2


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