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Volumn 23, Issue 1, 1999, Pages 1-11

FtsH - a single-chain charonin?

Author keywords

AAA family; Chaperone; Integral membrane protein; Protease; SpoVM; CII protein; 32

Indexed keywords

ALKALINE PHOSPHATASE; BACTERIAL PROTEIN; CHAPERONE; MEMBRANE PROTEIN; METALLOPROTEINASE; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; REGULATOR PROTEIN; SIGMA FACTOR;

EID: 0032965905     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-6445(98)00024-2     Document Type: Article
Times cited : (100)

References (50)
  • 1
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996) Molecular chaperones in cellular protein folding. Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 2
    • 0028979581 scopus 로고
    • Repair, refold, recycle: How bacteria can deal with spontaneous and environmental damage to proteins
    • Visick, J.E. and Clarke, S. (1995) Repair, refold, recycle: how bacteria can deal with spontaneous and environmental damage to proteins. Mol. Microbiol. 16, 835-845.
    • (1995) Mol. Microbiol. , vol.16 , pp. 835-845
    • Visick, J.E.1    Clarke, S.2
  • 3
    • 0025063386 scopus 로고
    • Microbial stress proteins
    • Watson, K. (1990) Microbial stress proteins. Adv. Microb. Physiol. 31, 183-223.
    • (1990) Adv. Microb. Physiol. , vol.31 , pp. 183-223
    • Watson, K.1
  • 4
    • 0029861722 scopus 로고    scopus 로고
    • ATP-dependent degradation of CcdA by Lon protease - Effects of secondary structure and heterologous subunit interactions
    • Van Melderen, L., Thi, M.H.D., Lecchi, P., Gottesman, S., Couturier, M. and Maurizi, M.R. (1996) ATP-dependent degradation of CcdA by Lon protease - Effects of secondary structure and heterologous subunit interactions. J. Biol. Chem. 271, 27730-27738.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27730-27738
    • Van Melderen, L.1    Thi, M.H.D.2    Lecchi, P.3    Gottesman, S.4    Couturier, M.5    Maurizi, M.R.6
  • 5
    • 0002356259 scopus 로고
    • Establishment of repressor synthesis
    • Hendrix, R.W., Roberts, J.W., Stahl, F.W. and Weisberg, R.A., Eds. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Wulff, D.L. and Rosenberg, M. (1983) Establishment of repressor synthesis. In: Lambda II (Hendrix, R.W., Roberts, J.W., Stahl, F.W. and Weisberg, R.A., Eds.) pp. 53-73. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1983) Lambda II , pp. 53-73
    • Wulff, D.L.1    Rosenberg, M.2
  • 6
    • 0016198523 scopus 로고
    • Fine structure mapping, complementation, and physiology of Escherichia coli hfl mutants
    • Gautsch, J.W. and Wulff, D.L. (1974) Fine structure mapping, complementation, and physiology of Escherichia coli hfl mutants. Genetics 77, 435-448.
    • (1974) Genetics , vol.77 , pp. 435-448
    • Gautsch, J.W.1    Wulff, D.L.2
  • 7
    • 0027436841 scopus 로고
    • The Escherichia coli hfla locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain
    • Noble, J.A., Innis, M.A., Koonin, E.V., Rudd, K.E., Banuett, F. and Herskowitz, I. (1993) The Escherichia coli hflA locus encodes a putative GTP-binding protein and two membrane proteins, one of which contains a protease-like domain. Proc. Natl. Acad. Sci. USA 90, 10866-10870.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10866-10870
    • Noble, J.A.1    Innis, M.A.2    Koonin, E.V.3    Rudd, K.E.4    Banuett, F.5    Herskowitz, I.6
  • 8
    • 0016627718 scopus 로고
    • Isolation and characterization of a new temperature-sensitive cell division mutant of Escherichia coli K-12
    • Santos, D. and Almeida, D.F. (1975) Isolation and characterization of a new temperature-sensitive cell division mutant of Escherichia coli K-12. J. Bacteriol. 124, 1502-1507.
    • (1975) J. Bacteriol. , vol.124 , pp. 1502-1507
    • Santos, D.1    Almeida, D.F.2
  • 10
    • 0021690597 scopus 로고
    • Escherichia coli K-12 tolZ mutants tolerant to colicins E2, E3, D, Ia, and Ib: Defect in generation of the electrochemical proton gradient
    • Matsuzawa, H., Ushiyama, S., Koyama, Y. and Ohta, T. (1984) Escherichia coli K-12 tolZ mutants tolerant to colicins E2, E3, D, Ia, and Ib: defect in generation of the electrochemical proton gradient. J. Bacteriol. 160, 733-739.
    • (1984) J. Bacteriol. , vol.160 , pp. 733-739
    • Matsuzawa, H.1    Ushiyama, S.2    Koyama, Y.3    Ohta, T.4
  • 12
    • 0031894053 scopus 로고    scopus 로고
    • Escherichia coli mrsC is an allele of hflB, encoding a membrane-associated ATPase and protease that is required for mRNa decay
    • Wang, R.F., O'Hara, E.B., Aldea, M., Bargmann, C.I., Gromley, H. and Kushner, S.R. (1998) Escherichia coli mrsC is an allele of hflB, encoding a membrane-associated ATPase and protease that is required for mRNA decay. J. Bacteriol. 180, 1929-1938.
    • (1998) J. Bacteriol. , vol.180 , pp. 1929-1938
    • Wang, R.F.1    O'Hara, E.B.2    Aldea, M.3    Bargmann, C.I.4    Gromley, H.5    Kushner, S.R.6
  • 13
    • 0027537133 scopus 로고
    • Isolation of stress mutants of Bacillus subtilis by a novel genetic method
    • Geisler, U. and Schumann, W. (1993) Isolation of stress mutants of Bacillus subtilis by a novel genetic method. FEMS Microbiol. Lett. 108, 251-254.
    • (1993) FEMS Microbiol. Lett. , vol.108 , pp. 251-254
    • Geisler, U.1    Schumann, W.2
  • 14
    • 0030978686 scopus 로고    scopus 로고
    • Characterization of the ftsH gene of Bacillus subtilis
    • Lysenko, E., Ogura, T. and Cutting, S.M. (1997) Characterization of the ftsH gene of Bacillus subtilis. Microbiology 143, 971-978.
    • (1997) Microbiology , vol.143 , pp. 971-978
    • Lysenko, E.1    Ogura, T.2    Cutting, S.M.3
  • 15
    • 0030700663 scopus 로고    scopus 로고
    • Characterization of anaerobic fermentative growth of Bacillus subtilis: Identification of fermentation end products and genes required for growth
    • Nakano, M.M., Dailly, Y.P., Zuber, P. and Clark, D.P. (1997) Characterization of anaerobic fermentative growth of Bacillus subtilis: Identification of fermentation end products and genes required for growth. J. Bacteriol. 179, 6749-6755.
    • (1997) J. Bacteriol. , vol.179 , pp. 6749-6755
    • Nakano, M.M.1    Dailly, Y.P.2    Zuber, P.3    Clark, D.P.4
  • 16
    • 0028853562 scopus 로고
    • Regulation of the heat-shock response depends on divalent metal ions in an hflB mutant of Escherichia coll
    • Herman, C., Lecat, S., D'Ari, R. and Bouloc, P. (1995) Regulation of the heat-shock response depends on divalent metal ions in an hflB mutant of Escherichia coll. Mol. Microbiol. 18, 247-256.
    • (1995) Mol. Microbiol. , vol.18 , pp. 247-256
    • Herman, C.1    Lecat, S.2    D'Ari, R.3    Bouloc, P.4
  • 17
    • 0028135021 scopus 로고
    • A Lactococcus lactis gene encodes a membrane protein with putative ATPase activity that is homologous to the essential Escherichia coli ftsH gene product
    • Nilsson, D., Lauridsen, A.A., Tomoyasu, T. and Ogura, T. (1994) A Lactococcus lactis gene encodes a membrane protein with putative ATPase activity that is homologous to the essential Escherichia coli ftsH gene product. Microbiology 140, 2601-2610.
    • (1994) Microbiology , vol.140 , pp. 2601-2610
    • Nilsson, D.1    Lauridsen, A.A.2    Tomoyasu, T.3    Ogura, T.4
  • 18
    • 10344231468 scopus 로고    scopus 로고
    • Sequencing, expression, and genetic characterization of the Helicobacter pylori ftsH gene encoding a protein homologous to members of a novel putative ATPase family
    • Ge, Z. and Taylor, D.E. (1996) Sequencing, expression, and genetic characterization of the Helicobacter pylori ftsH gene encoding a protein homologous to members of a novel putative ATPase family. J. Bacteriol. 178, 6151-6157.
    • (1996) J. Bacteriol. , vol.178 , pp. 6151-6157
    • Ge, Z.1    Taylor, D.E.2
  • 20
    • 0028840312 scopus 로고
    • FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli
    • Akiyama, Y., Yoshihisa, T. and Ito, K. (1995) FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 270, 23485-23490.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23485-23490
    • Akiyama, Y.1    Yoshihisa, T.2    Ito, K.3
  • 21
    • 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. and Ogura, T. (1993) 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, 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
  • 22
    • 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. and Ito, K. (1996) FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins. J. Biol. Chem. 271, 31196-31201.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31196-31201
    • Akiyama, Y.1    Kihara, A.2    Tokuda, H.3    Ito, K.4
  • 23
    • 0031803530 scopus 로고    scopus 로고
    • Polypeptide binding of Escherichia coli FtsH (HflB)
    • Akiyama, Y., Ehrmann, M., Kihara, A. and Ito, K. (1998) Polypeptide binding of Escherichia coli FtsH (HflB). Mol. Microbiol. 28, 803-812.
    • (1998) Mol. Microbiol. , vol.28 , pp. 803-812
    • Akiyama, Y.1    Ehrmann, M.2    Kihara, A.3    Ito, K.4
  • 24
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri, F. and Duguet, M. (1995) A 200-amino acid ATPase module in search of a basic function. BioEssays 17, 639-650.
    • (1995) BioEssays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 27
    • 0029074510 scopus 로고
    • The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshock
    • Deuerling, E., Paeslack, B. and Schumann, W. (1995) The ftsH gene of Bacillus subtilis is transiently induced after osmotic and temperature upshock. J. Bacteriol. 177, 4105-4112.
    • (1995) J. Bacteriol. , vol.177 , pp. 4105-4112
    • Deuerling, E.1    Paeslack, B.2    Schumann, W.3
  • 28
    • 0028821695 scopus 로고
    • The recA gene of Lactococcus lactis: Characterization and involvement in oxidative and thermal stress
    • Duwat, P., Ehrlich, S.D. and Gruss, A. (1995) The recA gene of Lactococcus lactis: characterization and involvement in oxidative and thermal stress. Mol. Microbiol. 17, 1121-1131.
    • (1995) Mol. Microbiol. , vol.17 , pp. 1121-1131
    • Duwat, P.1    Ehrlich, S.D.2    Gruss, A.3
  • 29
    • 0030741916 scopus 로고    scopus 로고
    • Identification and characterization of an operon of Helicobacter pylori that is involved in motility and stress adaptation
    • Beier, D., Spohn, G., Rappuoli, R. and Scarlato, V. (1997) Identification and characterization of an operon of Helicobacter pylori that is involved in motility and stress adaptation. J. Bacteriol. 179, 4676-4683.
    • (1997) J. Bacteriol. , vol.179 , pp. 4676-4683
    • Beier, D.1    Spohn, G.2    Rappuoli, R.3    Scarlato, V.4
  • 30
    • 0031900421 scopus 로고    scopus 로고
    • The Helicobacter felis ftsH gene encoding an ATP-dependent metalloprotease can replace the Escherichia coli homologue for growth and phage A, lysogenization
    • Melchers, K., Wiegert, T., Buhmann, A., Postius, S., Schäfer, K.P. and Schumann, W. (1998) The Helicobacter felis ftsH gene encoding an ATP-dependent metalloprotease can replace the Escherichia coli homologue for growth and phage A, lysogenization. Arch. Microbiol. 169, 393-396.
    • (1998) Arch. Microbiol. , vol.169 , pp. 393-396
    • Melchers, K.1    Wiegert, T.2    Buhmann, A.3    Postius, S.4    Schäfer, K.P.5    Schumann, W.6
  • 31
    • 0031033658 scopus 로고    scopus 로고
    • The ftsH gene of Bacillus subtilis is involved in major cellular processes such as sporulation, stress adaptation and secretion
    • Deuerling, E., Mogk, A., Richter, C., Purucker, M. and Schumann, W. (1997) The ftsH gene of Bacillus subtilis is involved in major cellular processes such as sporulation, stress adaptation and secretion. Mol. Microbiol. 23, 921-933.
    • (1997) Mol. Microbiol. , vol.23 , pp. 921-933
    • Deuerling, E.1    Mogk, A.2    Richter, C.3    Purucker, M.4    Schumann, W.5
  • 32
    • 0029910627 scopus 로고    scopus 로고
    • A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY
    • Kihara, A., Akiyama, Y. and Ito, K. (1996) A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY. EMBO J. 15, 6122-6131.
    • (1996) EMBO J. , vol.15 , pp. 6122-6131
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 33
    • 0032577263 scopus 로고    scopus 로고
    • Different pathways for protein degradation by the FtsH/HflKC membraneembedded protease complex: An implication from the interference by a mutant form of a new substrate protein, YccA
    • Kihara, A., Akiyama, Y. and Ito, K. (1998) Different pathways for protein degradation by the FtsH/HflKC membraneembedded protease complex: An implication from the interference by a mutant form of a new substrate protein, YccA. J. Mol. Biol. 279, 175-188.
    • (1998) J. Mol. Biol. , vol.279 , pp. 175-188
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 35
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • Kunst, F., Ogasawara, N., Moszer, I., Albertini, A.M., Alloni, G., Azevedo, V. et al. (1997) The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature 390, 249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4    Alloni, G.5    Azevedo, V.6
  • 38
    • 0030914642 scopus 로고    scopus 로고
    • Host regulation of lysogenic decision in bacteriophage lambda: Transmembrane modulation of FtsH (HflB), the ell degrading protease, by HflKC (HflA)
    • Kihara, A., Akiyama, Y. and Ito, K. (1997) Host regulation of lysogenic decision in bacteriophage lambda: Transmembrane modulation of FtsH (HflB), the ell degrading protease, by HflKC (HflA). Proc. Natl. Acad. Sci. USA 94, 5544-5549.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5544-5549
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 39
    • 2642666491 scopus 로고    scopus 로고
    • Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)
    • Herman, C., Thévenet, D., Bouloc, P., Walker, G.C. and D'Ari, R. (1998) Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH). Genes Dev. 12, 1348-1355.
    • (1998) Genes Dev. , vol.12 , pp. 1348-1355
    • Herman, C.1    Thévenet, D.2    Bouloc, P.3    Walker, G.C.4    D'Ari, R.5
  • 40
    • 0031036515 scopus 로고
    • The HflB protease of Escherichia coli degrades its inhibitor λcIII
    • Herman, C., Thévenet, D., D'Ari, R. and Bouloc, P. (1995) The HflB protease of Escherichia coli degrades its inhibitor λcIII. J. Bacteriol. 179, 358-363.
    • (1995) J. Bacteriol. , vol.179 , pp. 358-363
    • Herman, C.1    Thévenet, D.2    D'Ari, R.3    Bouloc, P.4
  • 41
    • 0027254541 scopus 로고
    • An unusually small gene required for sporulation by Bacillus subtilis
    • Levin, P.A., Fan, N., Ricca, E., Driks, A., Losick, R. and Cutting, S. (1993) An unusually small gene required for sporulation by Bacillus subtilis. Mol. Microbiol. 9, 761-771.
    • (1993) Mol. Microbiol. , vol.9 , pp. 761-771
    • Levin, P.A.1    Fan, N.2    Ricca, E.3    Driks, A.4    Losick, R.5    Cutting, S.6
  • 42
    • 0030928663 scopus 로고    scopus 로고
    • SpoVM, a small protein essential to development in Bacillus subtilis, interacts with the ATP-dependent protease FtsH
    • Cutting, S., Anderson, M., Lysenko, E., Page, A., Tomoyasu, T., Tatematsu, K., Tatsuta, T., Kroos, L. and Ogura, T. (1997) SpoVM, a small protein essential to development in Bacillus subtilis, interacts with the ATP-dependent protease FtsH. J. Bacteriol. 179, 5534-5542.
    • (1997) J. Bacteriol. , vol.179 , pp. 5534-5542
    • Cutting, S.1    Anderson, M.2    Lysenko, E.3    Page, A.4    Tomoyasu, T.5    Tatematsu, K.6    Tatsuta, T.7    Kroos, L.8    Ogura, T.9
  • 43
    • 0027983603 scopus 로고
    • Involvement of FtsH in protein assembly into and through the membrane. I. Mutations that reduce retention efficiency of a cytoplasmic reporter
    • Akiyama, Y., Ogura, T. and Ito, K. (1994) Involvement of FtsH in protein assembly into and through the membrane. I. Mutations that reduce retention efficiency of a cytoplasmic reporter. J. Biol. Chem. 269, 5218-5224.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5218-5224
    • Akiyama, Y.1    Ogura, T.2    Ito, K.3
  • 44
    • 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. (1995) FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit. Proc. Natl. Acad. Sci. USA 92, 4532-4536.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4532-4536
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 45
    • 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, 26-28.
    • (1996) FEBS Lett. , vol.399 , pp. 26-28
    • Akiyama, Y.1    Kihara, A.2    Ito, K.3
  • 46
    • 0030025784 scopus 로고    scopus 로고
    • Suppression of ftsH mutant phenotypes by overproduction of molecular chaperones
    • Shirai, Y., Akiyama, Y. and Ito, K. (1996) Suppression of ftsH mutant phenotypes by overproduction of molecular chaperones. J. Bacteriol. 178, 1141-1145.
    • (1996) J. Bacteriol. , vol.178 , pp. 1141-1145
    • Shirai, Y.1    Akiyama, Y.2    Ito, K.3
  • 48
    • 0030457111 scopus 로고    scopus 로고
    • Molecular genetics of sporulation in Bacillus subtilis
    • Stragier, P. and Losick, R. (1996) Molecular genetics of sporulation in Bacillus subtilis. Annu. Rev. Genet. 30, 297-341.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 297-341
    • Stragier, P.1    Losick, R.2
  • 49
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jacob, U., Gaestel, M., Engel, K. and Buchner, J. (1993) Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268, 1517-1520.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1517-1520
    • Jacob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 50
    • 0031894923 scopus 로고    scopus 로고
    • Lambda Xis degradation in vivo by Lon and FtsH
    • Leffers, G.G. and Gottesman, S. (1998) Lambda Xis degradation in vivo by Lon and FtsH. J. Bacteriol. 180, 1573-1577.
    • (1998) J. Bacteriol. , vol.180 , pp. 1573-1577
    • Leffers, G.G.1    Gottesman, S.2


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