메뉴 건너뛰기




Volumn 179, Issue 2, 1997, Pages 358-363

The HflB protease of Escherichia coli degrades its inhibitor λcIII

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE;

EID: 0031036515     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.2.358-363.1997     Document Type: Article
Times cited : (79)

References (49)
  • 1
    • 0029989855 scopus 로고    scopus 로고
    • FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins
    • Akiyama, Y., A. Kihara, H. Tokuda, and K. Ito. 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
  • 2
    • 0027983603 scopus 로고
    • Involvement of FtsH in protein assembly into and through the membrane. I. Mutations that reduce retention efficiency of a cyloplasmic reporter
    • Akiyama, Y., T. Ogura, and K. Ito. 1994. Involvement of FtsH in protein assembly into and through the membrane. I. Mutations that reduce retention efficiency of a cyloplasmic 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
  • 3
    • 0028033333 scopus 로고
    • Involvement of FtsH in protein assembly into and through the membrane. II. Dominant mutations a fleeting FtsH functions
    • Akiyama, Y., Y. Shirai, and K. Ito. 1994, Involvement of FtsH in protein assembly into and through the membrane. II. Dominant mutations a fleeting FtsH functions. J Biol. Chem. 269:5225-5229.
    • (1994) J Biol. Chem. , vol.269 , pp. 5225-5229
    • Akiyama, Y.1    Shirai, Y.2    Ito, K.3
  • 5
    • 0022477617 scopus 로고
    • HflB, a new Escherrichia coli locus regulating lysogeny and the level of bacteriophage lambda ell protein
    • Banuett, F., M. A. Hoyt, L. McFarlane, H. Echols, and I. Herskowitz, 1986. hflB, a new Escherrichia coli locus regulating lysogeny and the level of bacteriophage lambda ell protein. J. Mol. Biol. 187:213-224.
    • (1986) J. Mol. Biol. , vol.187 , pp. 213-224
    • Banuett, F.1    Hoyt, M.A.2    McFarlane, L.3    Echols, H.4    Herskowitz, I.5
  • 7
    • 0029037015 scopus 로고
    • Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication
    • Buchberger, A., H. Theyssen, H. Schroder, J. S. McCarty, G. Virgallita, P. Milkereit, J. Reinstein, and B. Bukau. 1995. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J. Biol. Chem. 270:16903-16910.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16903-16910
    • Buchberger, A.1    Theyssen, H.2    Schroder, H.3    McCarty, J.S.4    Virgallita, G.5    Milkereit, P.6    Reinstein, J.7    Bukau, B.8
  • 8
    • 0024110776 scopus 로고
    • Cleavage of the eII protein of phage lambda by purified HflA protease: Control of the switch between lysis and lysogeny
    • Cheng, H. H., P. J. Muhlrad, M. A. Hoyt, and H. Echols. 1988. Cleavage of the eII protein of phage lambda by purified HflA protease: control of the switch between lysis and lysogeny. Proc. Natl. Acad. Sci. USA 85:7882-7886.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7882-7886
    • Cheng, H.H.1    Muhlrad, P.J.2    Hoyt, M.A.3    Echols, H.4
  • 9
    • 0029328549 scopus 로고
    • A 200 amino acid-ATPase module in search for a basic function
    • Confalonieri, F., and M. Duguet. 1995. A 200 amino acid-ATPase module in search for a basic function. BioEssays 17:639-650.
    • (1995) BioEssays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 10
    • 0001035136 scopus 로고
    • Complete annotated lambda sequence
    • R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg (ed.), Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Daniels, D., J. Schroeder, W. Szybalski, F. Sanger, and F. Blattner. 1983. Complete annotated lambda sequence, p. 519-676. In R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg (ed.), Lambda II. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1983) Lambda II. , vol.2 , pp. 519-676
    • Daniels, D.1    Schroeder, J.2    Szybalski, W.3    Sanger, F.4    Blattner, F.5
  • 11
    • 15144355615 scopus 로고
    • Further phenotypic analysis of the cell division mutant Y16 of Escherichia coli K12
    • de Souza Ferreira, L. C., and D. F. de Almeida. 1984. Further phenotypic analysis of the cell division mutant Y16 of Escherichia coli K12. Rev. Brasil. Genet. VII:205-217.
    • (1984) Rev. Brasil. Genet. , vol.7 , pp. 205-217
    • De Souza Ferreira, L.C.1    De Almeida, D.F.2
  • 12
    • 0002501256 scopus 로고
    • Bacteriophage λ development: Temporal switches and the choices of lysis and lysogeny
    • Echols, H. 1986. Bacteriophage λ development: temporal switches and the choices of lysis and lysogeny. Trends Genet. 2:26-30.
    • (1986) Trends Genet. , vol.2 , pp. 26-30
    • Echols, H.1
  • 13
    • 0021709321 scopus 로고
    • Interaction of bacteriophage and host macromolecules in the growth of bacteriophage lambda
    • Friedman, D. I., E. R. Obson, D. Corven, and M. Gellert, 1984. Interaction of bacteriophage and host macromolecules in the growth of bacteriophage lambda. Microbiol. Rev. 48:299-325.
    • (1984) Microbiol. Rev. , vol.48 , pp. 299-325
    • Friedman, D.I.1    Obson, E.R.2    Corven, D.3    Gellert, M.4
  • 15
    • 0026454716 scopus 로고
    • Regulation by proteolysis: Energy-dependent proteases and their targets
    • Gottesman, S., and M. R. Maurizi. 1992. Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol. Rev. 56:592-621.
    • (1992) Microbiol. Rev. , vol.56 , pp. 592-621
    • Gottesman, S.1    Maurizi, M.R.2
  • 16
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., D. Belin, M. J. Carson, and J. Beckwith. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 17
    • 0028853562 scopus 로고
    • Regulation of the heat shock response depends on divalent metal ions in an hflB mutant of Escherichia coli
    • Herman, C., S. Lecat, R. D'Ari, and P. Bouloc. 1995. Regulation of the heat shock response depends on divalent metal ions in an hflB mutant of Escherichia coli. Mol. Microbiol. 18:247-255.
    • (1995) Mol. Microbiol. , vol.18 , pp. 247-255
    • Herman, C.1    Lecat, S.2    D'Ari, R.3    Bouloc, P.4
  • 21
    • 0020428339 scopus 로고
    • Control of phage λ development by stability and synthesis of the cII protein: Role of the viral cIII and host hflA, himA, and himD genes
    • Hoyt, M. A., D. M. Knight, A. Das, H. I. Miller, and H. Echols. 1982. Control of phage λ development by stability and synthesis of the cII protein: role of the viral cIII and host hflA, himA, and himD genes. Cell 31:565-573.
    • (1982) Cell , vol.31 , pp. 565-573
    • Hoyt, M.A.1    Knight, D.M.2    Das, A.3    Miller, H.I.4    Echols, H.5
  • 22
    • 0019829757 scopus 로고
    • An inducible DNA replication-cell division coupling mechanism in E. coli
    • Huisman, O., and R. D'Ari. 1981. An inducible DNA replication-cell division coupling mechanism in E. coli. Nature 290:797-799.
    • (1981) Nature , vol.290 , pp. 797-799
    • Huisman, O.1    D'Ari, R.2
  • 23
    • 0344321693 scopus 로고
    • Cell division control in Escherichia coli: Specific induction of the SOS function SfiA protein is sufficient to block septation
    • Huisman, O., R. D'Ari, and S. Gottesman. 1984. Cell division control in Escherichia coli: specific induction of the SOS function SfiA protein is sufficient to block septation. Proc. Natl. Acad. Sci. USA 81:4490-4494.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4490-4494
    • Huisman, O.1    D'Ari, R.2    Gottesman, S.3
  • 24
    • 0022633653 scopus 로고
    • Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing attachment sites between the inner and outer membranes and the murein skeleton of the cell envelope
    • Ishidate, K., E. S. Creeger, J. Zrike, S. Deb, B. Glauner, T. J. MacAlister, and L. I. Rothfield, 1986. Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing attachment sites between the inner and outer membranes and the murein skeleton of the cell envelope. J. Biol. Chem. 261:428-440.
    • (1986) J. Biol. Chem. , vol.261 , pp. 428-440
    • Ishidate, K.1    Creeger, E.S.2    Zrike, J.3    Deb, S.4    Glauner, B.5    MacAlister, T.J.6    Rothfield, L.I.7
  • 25
    • 0002738378 scopus 로고
    • Mutations in a temperate bacteriophage affecting its ability to lysogenize Escherichia coli
    • Kaiser, A. D. 1957. Mutations in a temperate bacteriophage affecting its ability to lysogenize Escherichia coli. Virology 3:42-61.
    • (1957) Virology , vol.3 , pp. 42-61
    • Kaiser, A.D.1
  • 26
    • 0028064780 scopus 로고
    • Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES
    • Kandror, O., L. Busconi, M. Sherman, and A. L. Goldberg. 1994. Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES. J. Biol. Chem. 269:23575-23582.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23575-23582
    • Kandror, O.1    Busconi, L.2    Sherman, M.3    Goldberg, A.L.4
  • 27
    • 0025955608 scopus 로고
    • The activity of the CIII regulator of lambdoid bacteriophages resides within a 24-amino acid protein domain
    • Kornitzer, D., S. Altuvia, and A. B. Oppenheim. 1991. The activity of the CIII regulator of lambdoid bacteriophages resides within a 24-amino acid protein domain. Proc. Natl. Acad. Sci. USA 88:5217-5221.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5217-5221
    • Kornitzer, D.1    Altuvia, S.2    Oppenheim, A.B.3
  • 28
    • 0024670902 scopus 로고
    • Genetic analysis of bacteriophage lambda cIII gene: MRNA structural requirements for translation initiation
    • Kornitzer, D., D. Teff, S. Altuvia, and A. B. Oppenheim. 1989. Genetic analysis of bacteriophage lambda cIII gene: mRNA structural requirements for translation initiation. J. Bacteriol. 171:2563-2572.
    • (1989) J. Bacteriol. , vol.171 , pp. 2563-2572
    • Kornitzer, D.1    Teff, D.2    Altuvia, S.3    Oppenheim, A.B.4
  • 29
    • 0027299142 scopus 로고
    • Two complementary approaches to study of peroxisome biogenesis in Saccharomyces cerevisiae: Forward and reverse genetics
    • Kunau, W. H., A. Beyer, T. Franken, K. Götte, M. Marzioch, J. Saidowsky, A. Skaletz-Rorowski, and F. F. Wiebel. 1993. Two complementary approaches to study of peroxisome biogenesis in Saccharomyces cerevisiae: forward and reverse genetics. Biochimie 75:209-224.
    • (1993) Biochimie , vol.75 , pp. 209-224
    • Kunau, W.H.1    Beyer, A.2    Franken, T.3    Götte, K.4    Marzioch, M.5    Saidowsky, J.6    Skaletz-Rorowski, A.7    Wiebel, F.F.8
  • 31
    • 0027954650 scopus 로고
    • DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: Expression of mutant DnaK proteins results in filamentation
    • McCarty, J. S., and G. C. Walker. 1994. DnaK mutants defective in ATPase activity are defective in negative regulation of the heat shock response: expression of mutant DnaK proteins results in filamentation. J. Bacteriol. 176:764-780.
    • (1994) J. Bacteriol. , vol.176 , pp. 764-780
    • McCarty, J.S.1    Walker, G.C.2
  • 32
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • McLaughlin, S., and A. Aderem. 1995. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20:272-276.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 33
    • 0025769565 scopus 로고
    • Role of heat shock protein DnaK in osmotic adaptation of Escherichia coli
    • Meury, J., and M. Kohiyama. 1991. Role of heat shock protein DnaK in osmotic adaptation of Escherichia coli. J. Bacteriol. 173:4404-4410.
    • (1991) J. Bacteriol. , vol.173 , pp. 4404-4410
    • Meury, J.1    Kohiyama, M.2
  • 35
    • 0026578696 scopus 로고
    • Detergent-shock response in enteric bacteria
    • Nickerson, K. W., and A. Aspedon. 1992. Detergent-shock response in enteric bacteria. Mol. Microbiol. 6:957-961.
    • (1992) Mol. Microbiol. , vol.6 , pp. 957-961
    • Nickerson, K.W.1    Aspedon, A.2
  • 36
    • 0018116010 scopus 로고
    • Studies of the energy requirement for intracellular protein degradation in Escherichia coli
    • Olden, K., and A. L. Goldberg. 1978. Studies of the energy requirement for intracellular protein degradation in Escherichia coli. Biochim. Biophys. Acta 542:385-398.
    • (1978) Biochim. Biophys. Acta , vol.542 , pp. 385-398
    • Olden, K.1    Goldberg, A.L.2
  • 37
    • 15144352897 scopus 로고    scopus 로고
    • Personal communication
    • 35a.Oppenheim, A. Personal communication.
    • Oppenheim, A.1
  • 38
    • 0023123175 scopus 로고
    • Escherichia coli dnaK null mutants are inviable at high temperature
    • Pack, K.-H., and G. C. Walker. 1987. Escherichia coli dnaK null mutants are inviable at high temperature. J. Bacteriol. 169:283-290.
    • (1987) J. Bacteriol. , vol.169 , pp. 283-290
    • Pack, K.-H.1    Walker, G.C.2
  • 41
    • 0023942606 scopus 로고
    • A bacteriophage T4 gene which functions to inhibit Escherichia coli Lon protease
    • Skorupski, K., J. Tomaschewski, W. Ruger, and L. D. Simon. 1988. A bacteriophage T4 gene which functions to inhibit Escherichia coli Lon protease. J. Bacteriol. 170:3016-3024.
    • (1988) J. Bacteriol. , vol.170 , pp. 3016-3024
    • Skorupski, K.1    Tomaschewski, J.2    Ruger, W.3    Simon, L.D.4
  • 43
    • 0020827719 scopus 로고
    • The DnaK protein modulates the heat-shock response of Escherichia coli
    • Tilly, K., N. McKittrick, M. Zylicz, and C. Georgopoulos. 1983. The DnaK protein modulates the heat-shock response of Escherichia coli. Cell 34:641-646.
    • (1983) Cell , vol.34 , pp. 641-646
    • Tilly, K.1    McKittrick, N.2    Zylicz, M.3    Georgopoulos, C.4
  • 47
    • 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., T. Yuki, S. Morimura, H. Mori, K. Yamanaka, H. Niki, S. Hiruga, and T. Ogura. 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    Hiruga, S.7    Ogura, T.8
  • 48
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira, J., and J. Messing. 1987. Production of single-stranded plasmid DNA. Methods Enzymol. 153:3-11.
    • (1987) Methods Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.