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Volumn 33, Issue 1, 1996, Pages 16-25

Effect of different temperature upshifts on protein synthesis by the psychrotrophic bacterium Pseudomonas fragi

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BACTERIAL GROWTH; DECOMPOSITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN SYNTHESIS; PSEUDOMONAS; TEMPERATURE SENSITIVITY;

EID: 0030007599     PISSN: 03438651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002849900067     Document Type: Article
Times cited : (12)

References (38)
  • 2
    • 0026314902 scopus 로고
    • Changes in rates of synthesis of individual proteins in a psychrophilic bacterium after a shift in temperature
    • Araki T (1991) Changes in rates of synthesis of individual proteins in a psychrophilic bacterium after a shift in temperature. Can J Microbiol 37:840-847
    • (1991) Can J Microbiol , vol.37 , pp. 840-847
    • Araki, T.1
  • 3
    • 0022863486 scopus 로고
    • Characterization of heat shock in Bacillus subtilis
    • Arnosti D, Singer V, Chamberlin MJ (1986) Characterization of heat shock in Bacillus subtilis. J Bacteriol 168:1243-1249
    • (1986) J Bacteriol , vol.168 , pp. 1243-1249
    • Arnosti, D.1    Singer, V.2    Chamberlin, M.J.3
  • 4
    • 0026663485 scopus 로고
    • Heat shock-induced protein synthesis in Lactococcus lactis subsp. lactis
    • Auffray Y, Gansel X, Thammavongs B, Boutibonnes P (1992) Heat shock-induced protein synthesis in Lactococcus lactis subsp. lactis. Curr Microbiol 24:281-284
    • (1992) Curr Microbiol , vol.24 , pp. 281-284
    • Auffray, Y.1    Gansel, X.2    Thammavongs, B.3    Boutibonnes, P.4
  • 5
    • 0001765941 scopus 로고
    • Stress proteins and thermotolerance in psychrotrophic yeasts from arctic environments
    • Berg GR, Inniss W, Barnum S (1993) Stress proteins and thermotolerance in psychrotrophic yeasts from arctic environments. Can J Microbiol 33:383-389
    • (1993) Can J Microbiol , vol.33 , pp. 383-389
    • Berg, G.R.1    Inniss, W.2    Barnum, S.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Chem 72:248-254
    • (1976) Anal Chem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0027319272 scopus 로고
    • Regulation of the Escherichia coli heat shock response
    • Bukau B (1993) Regulation of the Escherichia coli heat shock response. Mol Microbiol 9:671-680
    • (1993) Mol Microbiol , vol.9 , pp. 671-680
    • Bukau, B.1
  • 8
    • 0027186528 scopus 로고
    • Characterization of twenty-six new heat shock genes of Escherichia coli
    • Chuang S, Blattner F (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J Bacteriol 175:5242-5252
    • (1993) J Bacteriol , vol.175 , pp. 5242-5252
    • Chuang, S.1    Blattner, F.2
  • 9
    • 0026760910 scopus 로고
    • Heat and cold shock protein synthesis in arctic and temperate strains of rhizobia
    • Cloutier J, Prevost D, Nadeau P, Antoun H (1992) Heat and cold shock protein synthesis in arctic and temperate strains of rhizobia. Appl Environ Microbiol 58:2846-2853
    • (1992) Appl Environ Microbiol , vol.58 , pp. 2846-2853
    • Cloutier, J.1    Prevost, D.2    Nadeau, P.3    Antoun, H.4
  • 10
    • 0021005265 scopus 로고
    • Microbial and chemical changes in chill-stored red meats
    • Roberts TA, Skinner FA (ed) London: Academic Press
    • Dainty RH, Shaw BG, Roberts TA (1983) Microbial and chemical changes in chill-stored red meats. In: Roberts TA, Skinner FA (ed) Food microbiology: advances and prospects. London: Academic Press, pp 151-178
    • (1983) Food Microbiology: Advances and Prospects , pp. 151-178
    • Dainty, R.H.1    Shaw, B.G.2    Roberts, T.A.3
  • 11
    • 0028120804 scopus 로고
    • Increased synthesis of DnaK, GroEL, and GroES homologs by Francisella tularensis LVS in response to heat and hydrogen peroxide
    • Ericsson M, Tärnvik A, Kuoppa K, Sandström G, Sjöstedt A (1994) Increased synthesis of DnaK, GroEL, and GroES homologs by Francisella tularensis LVS in response to heat and hydrogen peroxide. Infect Immun 62:178-183
    • (1994) Infect Immun , vol.62 , pp. 178-183
    • Ericsson, M.1    Tärnvik, A.2    Kuoppa, K.3    Sandström, G.4    Sjöstedt, A.5
  • 12
    • 0024578552 scopus 로고
    • GroE heat shock proteins promote assembly of foreign prokaryotic ribulose biphosphate carboxylase oligomers in Escherichia coli
    • Goloubinoff P, Gatenby AA, Lorimer GH (1989) GroE heat shock proteins promote assembly of foreign prokaryotic ribulose biphosphate carboxylase oligomers in Escherichia coli. Nature 337:44-47
    • (1989) Nature , vol.337 , pp. 44-47
    • Goloubinoff, P.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 13
    • 15844364650 scopus 로고    scopus 로고
    • Hébraud M (1995) Unpublished data. C8.0 [=CapB], EMBL accession number P80415
    • Hébraud M (1995) Unpublished data. C8.0 [=CapB], EMBL accession number P80415
  • 14
    • 15844365200 scopus 로고
    • Characterization of two cold-shock like proteins from the psychrotropic bacterium, Pseudomonas fragi
    • Hancock REW (ed): Vancouver, British Columbia, Canada
    • Hébraud M, Anglade P, Ribadeau-Dumas B, Labadie J (1993) Characterization of two cold-shock like proteins from the psychrotropic bacterium, Pseudomonas fragi. In: Hancock REW (ed): Proceedings of the 4th international symposium on Pseudomonas. Vancouver, British Columbia, Canada: p57
    • (1993) Proceedings of the 4th International Symposium on Pseudomonas , pp. 57
    • Hébraud, M.1    Anglade, P.2    Ribadeau-Dumas, B.3    Labadie, J.4
  • 15
    • 0028198927 scopus 로고
    • Effect of growth temperatures on the protein levels in a psychrotrophic bacterium, Pseudomonas fragi
    • Hébraud M, Dubois E, Potier P, Labadie J (1994) Effect of growth temperatures on the protein levels in a psychrotrophic bacterium, Pseudomonas fragi. J Bacteriol 176:4017-4024
    • (1994) J Bacteriol , vol.176 , pp. 4017-4024
    • Hébraud, M.1    Dubois, E.2    Potier, P.3    Labadie, J.4
  • 16
    • 0028363836 scopus 로고
    • The cold-shock response - A hot topic
    • Jones PG, Inouye M (1994) The cold-shock response - a hot topic. Mol Microbiol 11:811-818
    • (1994) Mol Microbiol , vol.11 , pp. 811-818
    • Jones, P.G.1    Inouye, M.2
  • 17
    • 0026641172 scopus 로고
    • DNA gyrase, CS7.4, and the cold shock response in Escherichia coli
    • Jones PG, Krah R, Tafuri SR, Wolffe AP (1992) DNA gyrase, CS7.4, and the cold shock response in Escherichia coli. J Bacteriol 174:5798-5802
    • (1992) J Bacteriol , vol.174 , pp. 5798-5802
    • Jones, P.G.1    Krah, R.2    Tafuri, S.R.3    Wolffe, A.P.4
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0026769818 scopus 로고
    • RNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock domain
    • Landsman D (1992) RNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock domain. Nucleic Acids Res 20:2861-2864
    • (1992) Nucleic Acids Res , vol.20 , pp. 2861-2864
    • Landsman, D.1
  • 20
    • 0025790144 scopus 로고
    • Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS
    • La Teana A, Brandi A, Falconi M, Spurio R, Pon CL, Gualerzi CO (1991) Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS. Proc Natl Acad Sci USA 88:10907-10911
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10907-10911
    • La Teana, A.1    Brandi, A.2    Falconi, M.3    Spurio, R.4    Pon, C.L.5    Gualerzi, C.O.6
  • 21
    • 0028339430 scopus 로고
    • Family of the major cold-shock protein, CspA [CS7.4] of Escherichia coli, whose members show a high sequence similarity with the eukaryotic Y-box binding proteins
    • Lee S, Xie A, Jiang W, Etchegaray JP, Jones P, Inouye M (1994) Family of the major cold-shock protein, CspA [CS7.4] of Escherichia coli, whose members show a high sequence similarity with the eukaryotic Y-box binding proteins. Mol Microbiol 11:833-839
    • (1994) Mol Microbiol , vol.11 , pp. 833-839
    • Lee, S.1    Xie, A.2    Jiang, W.3    Etchegaray, J.P.4    Jones, P.5    Inouye, M.6
  • 23
    • 0017950371 scopus 로고
    • Transient rates of synthesis of individual polypeptides in Escherichia coli
    • Lemaux P, Herendeen S, Bloch P, Neidhardt F (1978) Transient rates of synthesis of individual polypeptides in Escherichia coli. Cell 13:427-434
    • (1978) Cell , vol.13 , pp. 427-434
    • Lemaux, P.1    Herendeen, S.2    Bloch, P.3    Neidhardt, F.4
  • 24
    • 0025374458 scopus 로고
    • Thermotolerance, cell filamentation and induced protein synthesis in psychrophilic and psychrotrophic bacteria
    • MacCallum KL, Inniss WE (1990) Thermotolerance, cell filamentation and induced protein synthesis in psychrophilic and psychrotrophic bacteria. Arch Microbiol 153:585-590
    • (1990) Arch Microbiol , vol.153 , pp. 585-590
    • MacCallum, K.L.1    Inniss, W.E.2
  • 25
    • 0022499287 scopus 로고
    • Temperature-dependent pattern of heat shock protein synthesis in psychrophilic and psychrotrophic microorganisms
    • MacCallum KL, Heikkila JJ, Inniss WE (1986) Temperature-dependent pattern of heat shock protein synthesis in psychrophilic and psychrotrophic microorganisms. Can J Microbiol 32:516-521
    • (1986) Can J Microbiol , vol.32 , pp. 516-521
    • MacCallum, K.L.1    Heikkila, J.J.2    Inniss, W.E.3
  • 26
    • 0003785155 scopus 로고
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory
    • Miller JH (1972) Experiments in molecular genetics. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory, pp 431-462
    • (1972) Experiments in Molecular Genetics , pp. 431-462
    • Miller, J.H.1
  • 27
    • 0000621735 scopus 로고
    • Heat shock response
    • Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE (ed) Washington DC: American Society for Microbiology
    • Neidhardt FC, VanBogelen RA (1987) Heat shock response. In: Neidhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, Umbarger HE (ed) Escherichia coli and Salmonella typhimurium: cellular and molecular biology. Washington DC: American Society for Microbiology, pp 1334-1345
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 1334-1345
    • Neidhardt, F.C.1    VanBogelen, R.A.2
  • 28
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell P (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250:4007-4021
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.1
  • 30
    • 0026437558 scopus 로고
    • The synthesis of cold-shock and cold acclimation proteins in the psychrotrophilic bacterium Aquaspirillum arcticum
    • Roberts M, Inniss WE (1992) The synthesis of cold-shock and cold acclimation proteins in the psychrotrophilic bacterium Aquaspirillum arcticum. Curr Microbiol 25:275-278
    • (1992) Curr Microbiol , vol.25 , pp. 275-278
    • Roberts, M.1    Inniss, W.E.2
  • 31
    • 0003275893 scopus 로고
    • Chilling, freezing and thawing
    • Brown MH (ed) London and New York: Applied Science Publishers Ltd
    • Rosset R (1982) Chilling, freezing and thawing. In: Brown MH (ed) Meat microbiology. London and New York: Applied Science Publishers Ltd, pp 265-318
    • (1982) Meat Microbiology , pp. 265-318
    • Rosset, R.1
  • 32
    • 0027296211 scopus 로고
    • Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
    • Schindelin H, Marahiel MA, Heinemann U (1993) Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature 364:164-168
    • (1993) Nature , vol.364 , pp. 164-168
    • Schindelin, H.1    Marahiel, M.A.2    Heinemann, U.3
  • 33
    • 0020827719 scopus 로고
    • The dnak protein modulates the heat-shock response of Escherichia coli
    • Tilly K, McKittrick N, Zylicz M, Georgopoulos C (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
  • 35
    • 0025804392 scopus 로고
    • Characterization of the heat shock response in Lactococcus lactis subsp. lactis
    • Whitaker RD, Batt CA (1991) Characterization of the heat shock response in Lactococcus lactis subsp. lactis. Appl Environ Microbiol 57:1408-1412
    • (1991) Appl Environ Microbiol , vol.57 , pp. 1408-1412
    • Whitaker, R.D.1    Batt, C.A.2
  • 36
    • 0027058752 scopus 로고
    • Cold shock proteins and cold acclimation proteins in a psychrotrophic bacterium
    • Whyte LG, Inniss WE (1992) Cold shock proteins and cold acclimation proteins in a psychrotrophic bacterium. Can J Microbiol 38:1281-1285
    • (1992) Can J Microbiol , vol.38 , pp. 1281-1285
    • Whyte, L.G.1    Inniss, W.E.2
  • 37
    • 0025776531 scopus 로고
    • Heat shock proteins and antigens of Mycobacterium tuberculosis
    • Young D, Garbe T (1991) Heat shock proteins and antigens of Mycobacterium tuberculosis. Infect Immun 59:3086-3093
    • (1991) Infect Immun , vol.59 , pp. 3086-3093
    • Young, D.1    Garbe, T.2
  • 38
    • 0021880465 scopus 로고
    • Purification and properties of the dnaJ replication protein of Escherichia coli
    • Zylics M, Yamamoto T, McKittrick N, Sell S, Georgopoulos C (1985) Purification and properties of the dnaJ replication protein of Escherichia coli. J Biol Chem 260:7591-7598
    • (1985) J Biol Chem , vol.260 , pp. 7591-7598
    • Zylics, M.1    Yamamoto, T.2    McKittrick, N.3    Sell, S.4    Georgopoulos, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.