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Volumn 180, Issue 10, 1998, Pages 2623-2629

The L-isoaspartyl protein repair methyltransferase enhances survival of aging Escherichia coli subjected to secondary environmental stresses

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTIC ACID; METHANOL; METHYLTRANSFERASE; OXYGEN RADICAL; PARAQUAT; SIGMA FACTOR; SODIUM CHLORIDE;

EID: 0031923137     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.10.2623-2629.1998     Document Type: Article
Times cited : (75)

References (34)
  • 1
    • 0026623463 scopus 로고
    • Examining the function and regulation of hsp 70 in cells subjected to metabolic stress
    • Beckmann, R. P., M. Lovett, and W. J. Welch. 1992. Examining the function and regulation of hsp 70 in cells subjected to metabolic stress. J. Cell Biol. 117:1137-1150.
    • (1992) J. Cell Biol. , vol.117 , pp. 1137-1150
    • Beckmann, R.P.1    Lovett, M.2    Welch, W.J.3
  • 2
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M. J., and S. N. Cohen. 1980. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138:179-207.
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 3
    • 0018850564 scopus 로고
    • Escherichia coli mutants with altered control of alcohol dehydrogenase and nitrate reductase
    • Clark, D., and J. E. Cronan, Jr. 1980. Escherichia coli mutants with altered control of alcohol dehydrogenase and nitrate reductase. J. Bacteriol. 141: 177-183.
    • (1980) J. Bacteriol. , vol.141 , pp. 177-183
    • Clark, D.1    Cronan Jr., J.E.2
  • 4
    • 0018700884 scopus 로고
    • Altered phospholipid composition in mutants of Escherichia coli sensitive or resistant to organic solvents
    • Clark, D. P., and J. P. Beard. 1979. Altered phospholipid composition in mutants of Escherichia coli sensitive or resistant to organic solvents. J. Gen. Microbiol. 113:267-274.
    • (1979) J. Gen. Microbiol. , vol.113 , pp. 267-274
    • Clark, D.P.1    Beard, J.P.2
  • 5
    • 0023464863 scopus 로고
    • Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins
    • Clarke, S. 1987. Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins. Int. J. Pept. Protein Res. 30:808-821.
    • (1987) Int. J. Pept. Protein Res. , vol.30 , pp. 808-821
    • Clarke, S.1
  • 6
    • 0023655449 scopus 로고
    • Protein damage and degradation by oxygen radicals. IV. Degradation of denatured proteins
    • Davies, K. J. A., S. W. Lin, and R. E. Pacific. 1987. Protein damage and degradation by oxygen radicals. IV. Degradation of denatured proteins. J. Biol. Chem. 262:9914-9920.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9914-9920
    • Davies, K.J.A.1    Lin, S.W.2    Pacific, R.E.3
  • 7
    • 0026769761 scopus 로고
    • New cloning vectors for integration into the λ attachment site attB of the Escherichia colimosome
    • Diederich, L., L. J. Rasmussen, and W. Messer. 1992. New cloning vectors for integration into the λ attachment site attB of the Escherichia colimosome. Plasmid 28:14-24.
    • (1992) Plasmid , vol.28 , pp. 14-24
    • Diederich, L.1    Rasmussen, L.J.2    Messer, W.3
  • 8
    • 0026316551 scopus 로고
    • Purification, gene cloning, and sequence analysis of an 1-isoaspartyi protein carhoxyl methyltransferase from Escherichia coli
    • Fu, J. C., L. Ding, and S. Clarke. 1991. Purification, gene cloning, and sequence analysis of an 1-isoaspartyi protein carhoxyl methyltransferase from Escherichia coli. J. Biol. Chem. 266:14562-14572.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14562-14572
    • Fu, J.C.1    Ding, L.2    Clarke, S.3
  • 9
    • 3242793191 scopus 로고
    • Direct clone characterization from plaques and colonies by the polymerase chain reaction
    • Gussow, D., and T. Clackson. 1989. Direct clone characterization from plaques and colonies by the polymerase chain reaction. Nucleic Acids Res. 17:4000.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4000
    • Gussow, D.1    Clackson, T.2
  • 10
    • 0018604132 scopus 로고
    • Paraquat and Escherichia coli
    • Hassan, H. M., and I. Fridovich. 1979. Paraquat and Escherichia coli. J. Biol. Chem. 254:10846-10852.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10846-10852
    • Hassan, H.M.1    Fridovich, I.2
  • 11
    • 0030995490 scopus 로고    scopus 로고
    • Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth, and fatal seizures in mice
    • Kim, E., J. D. Lowenson, D. C. MacLaren, S. Clarke, and S. G. Young. 1997. Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth, and fatal seizures in mice. Proc. Natl. Acad. Sci. USA 94:6132-6137.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6132-6137
    • Kim, E.1    Lowenson, J.D.2    MacLaren, D.C.3    Clarke, S.4    Young, S.G.5
  • 12
    • 0026661893 scopus 로고
    • A protein methyltransferase specific for altered aspartyl residues is important in Escherichia coli stationary-phase survival and heat-shock resistance
    • Li, C., and S. Clarke. 1992. A protein methyltransferase specific for altered aspartyl residues is important in Escherichia coli stationary-phase survival and heat-shock resistance. Proc. Natl. Acad. Sci. USA 89:9885-9889.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9885-9889
    • Li, C.1    Clarke, S.2
  • 13
    • 0028109045 scopus 로고
    • A new gene involved in stationary-phase survival located at 59 minutes on the Escherichia coli chromosome
    • Li, C., J. K. Ichikawa, J. J. Ravetto, H.-C. Kuo, J. C. Fu, and S. Clarke. 1994. A new gene involved in stationary-phase survival located at 59 minutes on the Escherichia coli chromosome. J. Bacteriol. 176:6015-6022.
    • (1994) J. Bacteriol. , vol.176 , pp. 6015-6022
    • Li, C.1    Ichikawa, J.K.2    Ravetto, J.J.3    Kuo, H.-C.4    Fu, J.C.5    Clarke, S.6
  • 15
    • 0021719208 scopus 로고
    • Genetic mapping of katF, a locus that with katE affects the synthesis of a second catalase species in Escherichia coli
    • Loewen, P. C., and B. L. Triggs. 1984. Genetic mapping of katF, a locus that with katE affects the synthesis of a second catalase species in Escherichia coli. J. Bacteriol. 160:668-675.
    • (1984) J. Bacteriol. , vol.160 , pp. 668-675
    • Loewen, P.C.1    Triggs, B.L.2
  • 17
    • 0008123901 scopus 로고
    • Conversion of isoaspartyl peptides to normal peptides by coupled enzymatic/nonenzymatic reactions: Implications for the cellular repair of damaged proteins
    • McFadden, P. N., and S. Clarke. 1987. Conversion of isoaspartyl peptides to normal peptides by coupled enzymatic/nonenzymatic reactions: implications for the cellular repair of damaged proteins. Proc. Natl. Acad. Sci. USA 84:2595-2599.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2595-2599
    • McFadden, P.N.1    Clarke, S.2
  • 18
    • 0028967490 scopus 로고
    • Escherichia coli peplide methionine sulfoxide reductase gene: Regulation of expression and role in protecting against oxidative damage
    • Moskovitz, J., M. A. Rahman, J. Strassman, S. O. Yancey, S. R. Kushner, N. Brot, and H. Weissbach. 1995. Escherichia coli peplide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage. J. Bacteriol. 177:502-507.
    • (1995) J. Bacteriol. , vol.177 , pp. 502-507
    • Moskovitz, J.1    Rahman, M.A.2    Strassman, J.3    Yancey, S.O.4    Kushner, S.R.5    Brot, N.6    Weissbach, H.7
  • 19
    • 0028150939 scopus 로고
    • Hormonal and environmental responsiveness of a developmentally regulated protein repair l-isoaspartyl methyltransferase in wheat
    • Mudgett, M. B., and S. Clarke. 1994. Hormonal and environmental responsiveness of a developmentally regulated protein repair l-isoaspartyl methyltransferase in wheat. J. Biol. Chem. 269:25605-25612.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25605-25612
    • Mudgett, M.B.1    Clarke, S.2
  • 20
    • 0024234806 scopus 로고
    • Cluning and physical characterization of katE and katF required for catalase HPII expression in Escherichia coli
    • Mulvey, M. R., P. A. Sorby, B. L. Triggs-Raine, and P. C. Loewen. 1988. Cluning and physical characterization of katE and katF required for catalase HPII expression in Escherichia coli. Gene 73:337-345.
    • (1988) Gene , vol.73 , pp. 337-345
    • Mulvey, M.R.1    Sorby, P.A.2    Triggs-Raine, B.L.3    Loewen, P.C.4
  • 21
    • 0024361230 scopus 로고
    • Protein denaturation during heat shock and related stress: Escherichia coli β-galactosidase and Photinus pyralis luciferase inactivation in mouse cells
    • Nguyen, V. T., M. Morange, and O. Bensaude. 1989. Protein denaturation during heat shock and related stress: Escherichia coli β-galactosidase and Photinus pyralis luciferase inactivation in mouse cells. J. Biol. Chem. 264: 10487-10492.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10487-10492
    • Nguyen, V.T.1    Morange, M.2    Bensaude, O.3
  • 22
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsed, D. A., and S. Lindquist. 1993. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27:437-496.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsed, D.A.1    Lindquist, S.2
  • 23
    • 0026523626 scopus 로고
    • Hsp104 is required for tolerance to many forms of stress
    • Sanchez, Y., J. Taulien, K. A. Borkovich, and S. Lindquist. 1992. Hsp104 is required for tolerance to many forms of stress. EMBO J. 11:2357-2364.
    • (1992) EMBO J. , vol.11 , pp. 2357-2364
    • Sanchez, Y.1    Taulien, J.2    Borkovich, K.A.3    Lindquist, S.4
  • 24
    • 0001332686 scopus 로고
    • Approaches to the study of survival and death in stationary-phase Escherichia coli
    • S. Kjelleberg (ed.), Plenum Press, New York, N.Y.
    • Siegele, D. A., M. Almirón, and R. Kolter. 1993. Approaches to the study of survival and death in stationary-phase Escherichia coli, p. 151-169. In S. Kjelleberg (ed.), Starvation in bacteria. Plenum Press, New York, N.Y.
    • (1993) Starvation in Bacteria , pp. 151-169
    • Siegele, D.A.1    Almirón, M.2    Kolter, R.3
  • 26
    • 0029926274 scopus 로고    scopus 로고
    • Positive selection vectors for allelic exchange
    • Skorupski, K., and R. K. Taylor. 1996. Positive selection vectors for allelic exchange. Gene 169:47-52.
    • (1996) Gene , vol.169 , pp. 47-52
    • Skorupski, K.1    Taylor, R.K.2
  • 27
    • 0014364651 scopus 로고
    • Protein degradation
    • Tanford, C. 1968. Protein degradation. Adv. Protein Chem. 23:121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 28
    • 0023129314 scopus 로고
    • Differential induction of heat shock, SOS, and oxidation stress regulons and accumulation of nucleotides in Escherichia coli
    • VanBogelen, R. A., P. M. Kelley, and F. C. Neidhardt. 1987. Differential induction of heat shock, SOS, and oxidation stress regulons and accumulation of nucleotides in Escherichia coli. J. Bacteriol. 169:26-32.
    • (1987) J. Bacteriol. , vol.169 , pp. 26-32
    • VanBogelen, R.A.1    Kelley, P.M.2    Neidhardt, F.C.3
  • 29
    • 0028783693 scopus 로고
    • Responses to toxicants of an Escherichia coli strain carrying a uspA′::lux genetic fusion and an E. coli strain carrying a grpE′::lux fusion are similar
    • Van Dyk, T. K., D. R. Smulski, T. R. Reed, S. Belkin, A. C. Vollmer, and R. A. LaRossa. 1995. Responses to toxicants of an Escherichia coli strain carrying a uspA′::lux genetic fusion and an E. coli strain carrying a grpE′::lux fusion are similar. Appl. Environ. Microbiol. 61:4124-4127.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4124-4127
    • Van Dyk, T.K.1    Smulski, D.R.2    Reed, T.R.3    Belkin, S.4    Vollmer, A.C.5    Larossa, R.A.6
  • 30
    • 0028979581 scopus 로고
    • Repair, refold, recycle: How bacteria can deal with spontaneous and environmental damage to proteins
    • Visick, J. E., and S. Clarke. 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
  • 31
    • 0030840083 scopus 로고    scopus 로고
    • RpoS- and OxyR-independent induction of HPI catalase at stationary phase in Escherichia coli and identification of rpoS mutations in common laboratory strains
    • Visick, J. E., and S. Clarke. 1997. RpoS- and OxyR-independent induction of HPI catalase at stationary phase in Escherichia coli and identification of rpoS mutations in common laboratory strains. J. Bacteriol. 179:4158-4163.
    • (1997) J. Bacteriol. , vol.179 , pp. 4158-4163
    • Visick, J.E.1    Clarke, S.2
  • 32
    • 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
  • 33
    • 0030602818 scopus 로고    scopus 로고
    • GASPing for life in stationary phase
    • Zambrano, M. M., and R. Kolter. 1996. GASPing for life in stationary phase. Cell 86:181-184.
    • (1996) Cell , vol.86 , pp. 181-184
    • Zambrano, M.M.1    Kolter, R.2
  • 34
    • 0027510647 scopus 로고
    • Microbial competition: Escherichia coli mutants that take over stationary phase cultures
    • Zambrano, M. M., D. A. Siegele, M. Almirón, A. Tormo, and R. Kolter. 1993. Microbial competition: Escherichia coli mutants that take over stationary phase cultures. Science 259:1757-1760.
    • (1993) Science , vol.259 , pp. 1757-1760
    • Zambrano, M.M.1    Siegele, D.A.2    Almirón, M.3    Tormo, A.4    Kolter, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.