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Volumn 181, Issue 12, 1999, Pages 3674-3680

The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; MALTOSE BINDING PROTEIN; MITOMYCIN C; PROTEINASE;

EID: 0033023919     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.12.3674-3680.1999     Document Type: Article
Times cited : (69)

References (47)
  • 1
    • 0024991124 scopus 로고
    • Analysis of ftsZ mutations that confer resistance to the cell division inhibitor SulA (SfiA)
    • Bi, E., and J. Lutkenhaus. 1990. Analysis of ftsZ mutations that confer resistance to the cell division inhibitor SulA (SfiA). J. Bacteriol. 172:5602-5609.
    • (1990) J. Bacteriol. , vol.172 , pp. 5602-5609
    • Bi, E.1    Lutkenhaus, J.2
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0027319272 scopus 로고
    • Regulation of the Escherichia coli heat-shock response
    • Bukau, B. 1993. Regulation of the Escherichia coli heat-shock response. Mol. Miciobiol. 9:671-680.
    • (1993) Mol. Miciobiol. , vol.9 , pp. 671-680
    • Bukau, B.1
  • 4
    • 0025597906 scopus 로고
    • Proteolysis and modulation of the activity of the cell division inhibitor SulA in Escherichia coli lon mutants
    • Canceill, D., E. Dervyn, and O. Huisman. 1990. Proteolysis and modulation of the activity of the cell division inhibitor SulA in Escherichia coli lon mutants. J. Bacteriol. 172:7297-7300.
    • (1990) J. Bacteriol. , vol.172 , pp. 7297-7300
    • Canceill, D.1    Dervyn, E.2    Huisman, O.3
  • 5
    • 0027445907 scopus 로고
    • Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli
    • Chuang, S.-E., V. Burland, G. Plunkett III, D. L. Daniels, and F. R. Blattner. 1993. Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli. Gene 134:1-6.
    • (1993) Gene , vol.134 , pp. 1-6
    • Chuang, S.-E.1    Burland, V.2    Plunkett G. III3    Daniels, D.L.4    Blattner, F.R.5
  • 6
    • 0020529422 scopus 로고
    • Characterisation of the promoter for the LexA regulated sulA gene of Escherichia coli
    • Cole, S. T. 1983. Characterisation of the promoter for the LexA regulated sulA gene of Escherichia coli. Mol. Gen. Genet. 189:400-404.
    • (1983) Mol. Gen. Genet. , vol.189 , pp. 400-404
    • Cole, S.T.1
  • 7
    • 0025967766 scopus 로고
    • Is hsp70 the cellular thermometer?
    • Craig, E. A., and C. A. Gross. 1991. Is hsp70 the cellular thermometer? Trends Biochem. Sci. 16:135-140.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 135-140
    • Craig, E.A.1    Gross, C.A.2
  • 8
    • 0028008820 scopus 로고
    • Mutations in ftsZ that confer resistance to SulA affect the interaction of FtsZ with GTP
    • Dai, K., A. Mukherjee, Y. Xu, and J. Lutkenhaus. 1994. Mutations in ftsZ that confer resistance to SulA affect the interaction of FtsZ with GTP. J. Bacteriol. 175:130-136.
    • (1994) J. Bacteriol. , vol.175 , pp. 130-136
    • Dai, K.1    Mukherjee, A.2    Xu, Y.3    Lutkenhaus, J.4
  • 9
    • 0020536519 scopus 로고
    • Proteins required for ultraviolet light and chemical mutagenesis
    • Elledge, S. J., and G. C. Walker. 1983. Proteins required for ultraviolet light and chemical mutagenesis. J. Mo. Bioll 164:175-192.
    • (1983) J. Mo. Bioll , vol.164 , pp. 175-192
    • Elledge, S.J.1    Walker, G.C.2
  • 10
    • 0017180426 scopus 로고
    • Second-site mutations in capR (lon) strains of Escherichia coli K-12 that prevent radiation sensitivity and allow bacteriophage lambda to lysogenize
    • Gayda, R. C., L. T. Yamamoto, and A. Markovitz. 1976. Second-site mutations in capR (lon) strains of Escherichia coli K-12 that prevent radiation sensitivity and allow bacteriophage lambda to lysogenize. J. Bacteriol. 127: 1208-1216.
    • (1976) J. Bacteriol. , vol.127 , pp. 1208-1216
    • Gayda, R.C.1    Yamamoto, L.T.2    Markovitz, A.3
  • 11
    • 0016816177 scopus 로고
    • Prophage induction and cell division in E. coli. III. Mutations sftA and sfiB restore division in tif and Ion strains and permit the expression of mutator properties of tif
    • George, J., M. Castellazzi, and G. Buttin. 1975. Prophage induction and cell division in E. coli. III. Mutations sftA and sfiB restore division in tif and Ion strains and permit the expression of mutator properties of tif. Mol. Gen. Genet. 140:309-332.
    • (1975) Mol. Gen. Genet. , vol.140 , pp. 309-332
    • George, J.1    Castellazzi, M.2    Buttin, G.3
  • 12
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman, S. 1996. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30:465-506.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 13
    • 0019842601 scopus 로고
    • Role of sulA and sulB in filamentation by Lon mutants of Escherichia coli K-12
    • Gottesman, S., E. Halpern, and P. Trisler. 1981. Role of sulA and sulB in filamentation by Lon mutants of Escherichia coli K-12. J. Bacteriol. 148:265-273.
    • (1981) J. Bacteriol. , vol.148 , pp. 265-273
    • Gottesman, S.1    Halpern, E.2    Trisler, P.3
  • 14
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman, S., E. Roche, Y.-N. Zhou, and R. T. Sauer. 1998. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12:1338-1347.
    • (1998) Genes Dev. , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.-N.3    Sauer, R.T.4
  • 15
    • 0001241680 scopus 로고    scopus 로고
    • Function and regulation of the heat shock proteins
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, D.C.
    • Gross, C A. 1996. Function and regulation of the heat shock proteins, p. 1382-1399. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 1382-1399
    • Gross, C.A.1
  • 16
    • 2642666491 scopus 로고    scopus 로고
    • Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)
    • Herman, C., D. Thevenet, P. Bouloc, G. C. Walker, and R. D'Ari. 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    Thevenet, D.2    Bouloc, P.3    Walker, G.C.4    D'Ari, R.5
  • 18
    • 0028916242 scopus 로고
    • A cell division inhibitor SulA of Escherichia coli directly interacts with FtsZ through GTP hydrolysis
    • Higashitani, A., N. Higashitani, and K. Horiuchi. 1995. A cell division inhibitor SulA of Escherichia coli directly interacts with FtsZ through GTP hydrolysis. Biochem. Biophys. Res. Commun. 209:198-204.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 198-204
    • Higashitani, A.1    Higashitani, N.2    Horiuchi, K.3
  • 19
    • 0030943075 scopus 로고    scopus 로고
    • Functional dissection of a cell-division inhibitor, SulA, of Escherichia coli and its negative regulation by Lon
    • Higashitani, A., Y. Ishii, Y. Kato, and K. Horiuchi. 1997. Functional dissection of a cell-division inhibitor, SulA, of Escherichia coli and its negative regulation by Lon. Mol. Gen. Genet. 254:351-357.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 351-357
    • Higashitani, A.1    Ishii, Y.2    Kato, Y.3    Horiuchi, K.4
  • 20
    • 0029789075 scopus 로고    scopus 로고
    • Interaction between FtsZ and inhibitors of cell division
    • Huang, J., C. Cao, and J. Lutkenhaus. 1996. Interaction between FtsZ and inhibitors of cell division. J. Bacteriol. 178:5080-5085.
    • (1996) J. Bacteriol. , vol.178 , pp. 5080-5085
    • Huang, J.1    Cao, C.2    Lutkenhaus, J.3
  • 21
    • 0019119526 scopus 로고
    • Further characterization of sftA and sfiB mutations in Escherichia coli
    • Huisman, O., R. D'Ari, and J. George. 1980. Further characterization of sftA and sfiB mutations in Escherichia coli. J. Bacteriol. 144:185-191.
    • (1980) J. Bacteriol. , vol.144 , pp. 185-191
    • Huisman, O.1    D'Ari, R.2    George, J.3
  • 22
    • 0017683494 scopus 로고
    • Fine structure mapping and properties of mutations suppressing the Ion mutation in Escherichia coli K-12 and B strains
    • Johnson, B. F. 1977. Fine structure mapping and properties of mutations suppressing the Ion mutation in Escherichia coli K-12 and B strains. Genet. Res. 30:273-286.
    • (1977) Genet. Res. , vol.30 , pp. 273-286
    • Johnson, B.F.1
  • 23
    • 0029828865 scopus 로고    scopus 로고
    • Role of the heat shock protein DnaJ in the Lon-dependent degradation of naturally unstable proteins
    • Jubete, Y., M. R. Maurizi, and S. Gottesman. 1996. Role of the heat shock protein DnaJ in the Lon-dependent degradation of naturally unstable proteins. J. Biol. Chem. 271:30798-30803.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30798-30803
    • Jubete, Y.1    Maurizi, M.R.2    Gottesman, S.3
  • 24
    • 0344187470 scopus 로고    scopus 로고
    • Unpublished data
    • Kanemori, M. Unpublished data.
    • Kanemori, M.1
  • 26
    • 0030566824 scopus 로고    scopus 로고
    • Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY
    • Kessel, M., W. Wu, S. Gottesman, E. Kocsis, A. C. Steven, and M. R. Maurizi. 1996. Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. FEBS Lett. 398:274-278.
    • (1996) FEBS Lett. , vol.398 , pp. 274-278
    • Kessel, M.1    Wu, W.2    Gottesman, S.3    Kocsis, E.4    Steven, A.C.5    Maurizi, M.R.6
  • 27
    • 0031559883 scopus 로고    scopus 로고
    • Overexpression of the hslVU operon suppresses SOS-mediated inhibition of cell division in Escherichia coli
    • Khattar, M. M. 1997. Overexpression of the hslVU operon suppresses SOS-mediated inhibition of cell division in Escherichia coli. FEBS Lett. 414:402-404.
    • (1997) FEBS Lett. , vol.414 , pp. 402-404
    • Khattar, M.M.1
  • 28
    • 0023669069 scopus 로고
    • The physical map of the whole Escherichia coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., K. Akiyama, and K. Isono. 1987. The physical map of the whole Escherichia coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50:495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 29
    • 0031894923 scopus 로고    scopus 로고
    • Lambda Xis degradation in vivo by Lon and FtsH
    • Leffers, G. G., Jr., and S. Gottesman. 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., Jr.1    Gottesman, S.2
  • 30
    • 0020608087 scopus 로고
    • Coupling of DNA replication and cell division: sulB is an allele of ftsZ
    • Lutkenhaus, J. F. 1983. Coupling of DNA replication and cell division: sulB is an allele of ftsZ. J. Bacteriol. 154:1339-1346.
    • (1983) J. Bacteriol. , vol.154 , pp. 1339-1346
    • Lutkenhaus, J.F.1
  • 31
    • 0030462757 scopus 로고    scopus 로고
    • Identification and characterization of HslV HslU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli
    • Missiakas, D., F. Schwager, J.-M. Betton, C. Georgopoulos, and S. Raina. 1996. Identification and characterization of HslV HslU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. EMBO J. 15:6899-6909.
    • (1996) EMBO J. , vol.15 , pp. 6899-6909
    • Missiakas, D.1    Schwager, F.2    Betton, J.-M.3    Georgopoulos, C.4    Raina, S.5
  • 32
    • 0020651799 scopus 로고
    • Protein degradation in Escherichia coli: The lon gene controls the stability of SulA protein
    • Mizusawa, S, and S. Gottesman. 1983. Protein degradation in Escherichia coli: the lon gene controls the stability of SulA protein. Proc. Natl. Acad. Sci. USA 80:358-362.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 358-362
    • Mizusawa, S.1    Gottesman, S.2
  • 36
    • 0029067887 scopus 로고
    • Overproduction and purification of SulA fusion protein in Escherichia coli and its degradation by Lon protease in vitro
    • Sonezaki, S., Y. Ishii, K. Okita, T. Sugino, A. Kondo, and Y. Kato. 1995. Overproduction and purification of SulA fusion protein in Escherichia coli and its degradation by Lon protease in vitro. Appl. MicrobioJ. Biotechnol. 43:304-309.
    • (1995) Appl. Microbioj. Biotechnol. , vol.43 , pp. 304-309
    • Sonezaki, S.1    Ishii, Y.2    Okita, K.3    Sugino, T.4    Kondo, A.5    Kato, Y.6
  • 37
    • 0024226522 scopus 로고
    • Escherichia coli heat shock gene mutants are defective in proteolysis
    • Straus, D. B., W. A. Walter, and C. A. Gross. 1988. Escherichia coli heat shock gene mutants are defective in proteolysis. Genes Dev. 2:1851-1858.
    • (1988) Genes Dev. , vol.2 , pp. 1851-1858
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 39
    • 0021253583 scopus 로고
    • Isolation and physical mapping of temperature-sensitive mutants defective in heat-shock induction of proteins in Escherichia coli
    • Tobe, T., K. Ito, and T. Yura. 1984. Isolation and physical mapping of temperature-sensitive mutants defective in heat-shock induction of proteins in Escherichia coli. Mol. Gen. Genet. 195:10-16.
    • (1984) Mol. Gen. Genet. , vol.195 , pp. 10-16
    • Tobe, T.1    Ito, K.2    Yura, T.3
  • 41
    • 0023131531 scopus 로고
    • Capsule synthesis in Escherichia coli K-12 is regulated by proteolysis
    • Torres-Cabassa, A. S., and S. Gottesman. 1987. Capsule synthesis in Escherichia coli K-12 is regulated by proteolysis. J. Bacteriol. 169:981-989.
    • (1987) J. Bacteriol. , vol.169 , pp. 981-989
    • Torres-Cabassa, A.S.1    Gottesman, S.2
  • 42
    • 0001078874 scopus 로고    scopus 로고
    • The SOS response of Escherichia coli
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), ASM Press, Washington, D.C.
    • Walker, G. C. 1996. The SOS response of Escherichia coli, p. 1400-1416. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 1400-1416
    • Walker, G.C.1
  • 43
    • 0029000134 scopus 로고
    • The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
    • Wawrzynow, A., D. Wojtkowiak, J. Marszalek, B. Banecki, M. Jonsen, B. Graves, C. Georgopoulos, and M. Zylicz. 1995. The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 14:1867-1877.
    • (1995) EMBO J. , vol.14 , pp. 1867-1877
    • Wawrzynow, A.1    Wojtkowiak, D.2    Marszalek, J.3    Banecki, B.4    Jonsen, M.5    Graves, B.6    Georgopoulos, C.7    Zylicz, M.8
  • 44
    • 0021361667 scopus 로고
    • Gratuitous repression of avtA in Escherichia coli and Salmonella typhimurium
    • Whalen, W. A., and C. M. Berg. 1984. Gratuitous repression of avtA in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 158:571-574.
    • (1984) J. Bacteriol. , vol.158 , pp. 571-574
    • Whalen, W.A.1    Berg, C.M.2
  • 45
    • 0033016759 scopus 로고    scopus 로고
    • Redundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV protease
    • Wu, W.-F., Y. Zhou, and S. Gottesman. 1999. Redundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV protease. J. Bacteriol. 181:3681-3687.
    • (1999) J. Bacteriol. , vol.181 , pp. 3681-3687
    • Wu, W.-F.1    Zhou, Y.2    Gottesman, S.3
  • 46
    • 0001588962 scopus 로고    scopus 로고
    • Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli
    • Yoo, S. J., J. H. Seol, D. H. Shin, M. Rohrwild, M.-S. Kang, K. Tanaka, A. L. Goldberg, and C. H. Chung. 1996. Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli. J. Biol. Chem. 271:14035-14040.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14035-14040
    • Yoo, S.J.1    Seol, J.H.2    Shin, D.H.3    Rohrwild, M.4    Kang, M.-S.5    Tanaka, K.6    Goldberg, A.L.7    Chung, C.H.8
  • 47
    • 0027385183 scopus 로고
    • Regulation of heat shock response in bacteria
    • Yura, T., H. Nagal, and H. Mori. 1993. Regulation of heat shock response in bacteria. Annu. Rev. Microbiol. 47:321-350.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 321-350
    • Yura, T.1    Nagal, H.2    Mori, H.3


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