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Volumn 69, Issue 4, 2003, Pages 2365-2371

Heat shock response by the hyperthermophilic archaeon Pyrococcus furiosus

Author keywords

[No Author keywords available]

Indexed keywords

DNA; GENES; POLYPEPTIDES;

EID: 0037393082     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.69.4.2365-2371.2003     Document Type: Article
Times cited : (97)

References (44)
  • 1
    • 0035370872 scopus 로고    scopus 로고
    • Global gene expression during short term ethanol stress in Saccharomyces cerevisiae
    • Alexandre, H., V. Ansanay-Galeote, S. Dequin, and B. Blondin. 2001. Global gene expression during short term ethanol stress in Saccharomyces cerevisiae. FEBS Lett. 498:98-103.
    • (2001) FEBS Lett. , vol.498 , pp. 98-103
    • Alexandre, H.1    Ansanay-Galeote, V.2    Dequin, S.3    Blondin, B.4
  • 2
    • 0031038205 scopus 로고    scopus 로고
    • Purification and characterization of a proteasome from the hyperthermophilic archaeon Pyrococcus furiosus
    • Bauer, M. W., S. H. Bauer, and R. M. Kelly. 1997. Purification and characterization of a proteasome from the hyperthermophilic archaeon Pyrococcus furiosus. Appl. Environ. Microbiol. 63:1160-1164.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1160-1164
    • Bauer, M.W.1    Bauer, S.H.2    Kelly, R.M.3
  • 3
    • 0032102006 scopus 로고    scopus 로고
    • Transcription and translation in archaea: A mosaic of eukaryl and bacterial features
    • Bell, S. D., and S. P. Jackson. 1998. Transcription and translation in archaea: a mosaic of eukaryl and bacterial features. Trends Microbiol. 6:222-228.
    • (1998) Trends Microbiol. , vol.6 , pp. 222-228
    • Bell, S.D.1    Jackson, S.P.2
  • 4
    • 0029562758 scopus 로고
    • A putative SOS repair gene (dinF-like) in a hyperthermophilic archaeon
    • Bouyoub, A., G. Barbier, J. Querellou, and P. Forterre. 1995. A putative SOS repair gene (dinF-like) in a hyperthermophilic archaeon. Gene 167:147-149.
    • (1995) Gene , vol.167 , pp. 147-149
    • Bouyoub, A.1    Barbier, G.2    Querellou, J.3    Forterre, P.4
  • 5
    • 2542509024 scopus 로고    scopus 로고
    • Role of trehalose in growth at high temperature of Salmonella enterica serovar Typhimurium
    • Canovas, D., S. A. Fletcher, M. Hayashi, and L. N. Csonka. 2001. Role of trehalose in growth at high temperature of Salmonella enterica serovar Typhimurium. J. Bacteriol. 183:3365-3371.
    • (2001) J. Bacteriol. , vol.183 , pp. 3365-3371
    • Canovas, D.1    Fletcher, S.A.2    Hayashi, M.3    Csonka, L.N.4
  • 6
    • 0036154307 scopus 로고    scopus 로고
    • Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides
    • Chhabra, S. R., K. R. Shockley, D. E. Ward, and R. M. Kelly. 2002. Regulation of endo-acting glycosyl hydrolases in the hyperthermophilic bacterium Thermotoga maritima grown on glucan- and mannan-based polysaccharides. Appl. Environ. Microbiol. 68:545-554.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 545-554
    • Chhabra, S.R.1    Shockley, K.R.2    Ward, D.E.3    Kelly, R.M.4
  • 7
    • 0037045396 scopus 로고    scopus 로고
    • Effect of heat stress on promoter binding by transcription factors in the cytosol of the archaeon Methanosarcina mazei
    • De Biase, A., A. J. L. Macario, and E. C. de Macario. 2002. Effect of heat stress on promoter binding by transcription factors in the cytosol of the archaeon Methanosarcina mazei. Gene 282:189-197.
    • (2002) Gene , vol.282 , pp. 189-197
    • De Biase, A.1    Macario, A.J.L.2    De Macario, E.C.3
  • 8
    • 0033083967 scopus 로고    scopus 로고
    • Proteasomes and other self-compartmentalizing proteases in prokaryotes
    • De Mot, R., I. Nagy, J. Walz, and W. Baumeister. 1999. Proteasomes and other self-compartmentalizing proteases in prokaryotes. Trends Microbiol. 7:88-92.
    • (1999) Trends Microbiol. , vol.7 , pp. 88-92
    • De Mot, R.1    Nagy, I.2    Walz, J.3    Baumeister, W.4
  • 9
    • 0022445886 scopus 로고
    • Pyrococcus furiosus sp. nov represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100° C
    • Fiala, G., and K. O. Stetter. 1986. Pyrococcus furiosus sp. nov represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100° C. Arch. Microbiol. 145:56-61.
    • (1986) Arch. Microbiol. , vol.145 , pp. 56-61
    • Fiala, G.1    Stetter, K.O.2
  • 10
    • 0036283446 scopus 로고    scopus 로고
    • A membrane-bound archaeal Lon protease displays ATP-independent proteolytic activity, towards unfolded proteins and ATP-dependent activity for folded proteins
    • Fukui, T., T. Egushi, H. Atomi, and T. Imanaka. 2002. A membrane-bound archaeal Lon protease displays ATP-independent proteolytic activity, towards unfolded proteins and ATP-dependent activity for folded proteins. J. Bacteriol. 184:3689-3698.
    • (2002) J. Bacteriol. , vol.184 , pp. 3689-3698
    • Fukui, T.1    Egushi, T.2    Atomi, H.3    Imanaka, T.4
  • 11
    • 0034141782 scopus 로고    scopus 로고
    • Prediction of transcription regulatory sites in archaea by a comparative genomic approach
    • Gelfand, M. S., E. V. Koonin, and A. A. Mirinov. 2000. Prediction of transcription regulatory sites in archaea by a comparative genomic approach. Nucleic Acids Res. 28:695-705.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 695-705
    • Gelfand, M.S.1    Koonin, E.V.2    Mirinov, A.A.3
  • 12
    • 0032825282 scopus 로고    scopus 로고
    • The janus face of the archaeal Cdc48/p97 homologue VAT: Protein folding versus unfolding
    • Golbik, R., A. N. Lupas, K. K. Koretke, W. Baumeister, and J. Peters. 1999. The janus face of the archaeal Cdc48/p97 homologue VAT: protein folding versus unfolding. Biol. Chem. 380:1049-1062.
    • (1999) Biol. Chem. , vol.380 , pp. 1049-1062
    • Golbik, R.1    Lupas, A.N.2    Koretke, K.K.3    Baumeister, W.4    Peters, J.5
  • 13
    • 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
  • 14
    • 0030944688 scopus 로고    scopus 로고
    • Acquired thermotolerance and stressed-phase growth of the extremely thermoacidophilic archaeon Metallospaera sedula in continuous culture
    • Han, C. J., S. H. Park, and R. M. Kelly. 1997. Acquired thermotolerance and stressed-phase growth of the extremely thermoacidophilic archaeon Metallospaera sedula in continuous culture. Appl. Environ. Microbiol. 63:2391-2396.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2391-2396
    • Han, C.J.1    Park, S.H.2    Kelly, R.M.3
  • 15
    • 0242652827 scopus 로고    scopus 로고
    • Online
    • Hasseman, J. 2001. TIGR microarray protocols. [Online.] http://www.tigr .org/tdb/microarray/protocolsTIGR.shtml.
    • (2001)
    • Hasseman, J.1
  • 17
    • 0028054926 scopus 로고
    • The role of trehalose synthesis for the acquisition of thermotolerance in yeast. II. Physiological concentrations of trehalose increase the thermal stability of proteins in vitro
    • Hottiger, T., C. De Virgilio, M. Hall, T. Boiler, and A. Wiemken. 1994. The role of trehalose synthesis for the acquisition of thermotolerance in yeast. II. Physiological concentrations of trehalose increase the thermal stability of proteins in vitro. Eur. J. Biochem. 15:187-193.
    • (1994) Eur. J. Biochem. , vol.15 , pp. 187-193
    • Hottiger, T.1    De Virgilio, C.2    Hall, M.3    Boiler, T.4    Wiemken, A.5
  • 19
    • 0032560551 scopus 로고    scopus 로고
    • The thermosome: Archetype of group II chaperonins
    • Klumpp, M., and W. Baumeister. 1998. The thermosome: archetype of group II chaperonins. FEBS Lett. 430:73-77.
    • (1998) FEBS Lett. , vol.430 , pp. 73-77
    • Klumpp, M.1    Baumeister, W.2
  • 21
    • 0034745504 scopus 로고    scopus 로고
    • Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach
    • Koonin, E. V., Y. I. Wolf, and L. Aravind. 2001. Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach. Genome Res. 11:240-252.
    • (2001) Genome Res. , vol.11 , pp. 240-252
    • Koonin, E.V.1    Wolf, Y.I.2    Aravind, L.3
  • 23
    • 0034889286 scopus 로고    scopus 로고
    • Regulation and mechanism of action of the small heat shock protein from the hyperthermophilic archaeon Pyrococcus furiosus
    • Laksanalamai, P., D. L. Maeder, and F. T. Robb. 2001. Regulation and mechanism of action of the small heat shock protein from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 183:5198-5202.
    • (2001) J. Bacteriol. , vol.183 , pp. 5198-5202
    • Laksanalamai, P.1    Maeder, D.L.2    Robb, F.T.3
  • 24
    • 0031662628 scopus 로고    scopus 로고
    • Effects of temperature, salinity, and medium composition on compatible solute accumulation by Thermococcus spp
    • Lamosa, P., L. O. Martins, M. S. Da Costa, and H. Santos. 1998. Effects of temperature, salinity, and medium composition on compatible solute accumulation by Thermococcus spp. Appl. Environ. Microbiol. 64:3591-3598.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3591-3598
    • Lamosa, P.1    Martins, L.O.2    Da Costa, M.S.3    Santos, H.4
  • 26
    • 0344500848 scopus 로고    scopus 로고
    • The archaeal molecular chaperone machine: Peculiarities and paradoxes
    • Macario, A. J. L., and E. C. de Macario. 1999. The archaeal molecular chaperone machine: peculiarities and paradoxes. Genetics 152:1277-1283.
    • (1999) Genetics , vol.152 , pp. 1277-1283
    • Macario, A.J.L.1    De Macario, E.C.2
  • 27
    • 0035260487 scopus 로고    scopus 로고
    • The molecular chaperone system and other anti-stress mechanisms in archaea
    • Macario, A. J. L., and E. C. de Macario. 2001. The molecular chaperone system and other anti-stress mechanisms in archaea. Front. Biosci. 6:D262-D283.
    • (2001) Front. Biosci. , vol.6
    • Macario, A.J.L.1    De Macario, E.C.2
  • 28
    • 0028981456 scopus 로고
    • Accumulation of mannosylglycerate and di-myo-inositol-phosphate by Pyrococcus furious in response to salinity and temperature
    • Martins, L. O., and H. Santos. 1995. Accumulation of mannosylglycerate and di-myo-inositol-phosphate by Pyrococcus furious in response to salinity and temperature. Appl. Environ. Microbiol. 61:3299-3303.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3299-3303
    • Martins, L.O.1    Santos, H.2
  • 29
  • 30
    • 0024110669 scopus 로고
    • A role for glyceraldehyde-3-phosphate dehydrogenase in the development of thermotolerance in Xenopus laevis embryos
    • Nickells, R. W., and L. W. Browder. 1988. A role for glyceraldehyde-3-phosphate dehydrogenase in the development of thermotolerance in Xenopus laevis embryos. J. Cell Biol. 107:1901-1909.
    • (1988) J. Cell Biol. , vol.107 , pp. 1901-1909
    • Nickells, R.W.1    Browder, L.W.2
  • 31
    • 0032549642 scopus 로고    scopus 로고
    • Proteasome function is dispensable under normal but not under heat shock conditions in Thermoplasma acidophilum
    • Ruepp, A., C. Eckerskorn, M. Bogyo, and W. Baumeister. 1998. Proteasome function is dispensable under normal but not under heat shock conditions in Thermoplasma acidophilum. FEBS Lett. 425:87-90.
    • (1998) FEBS Lett. , vol.425 , pp. 87-90
    • Ruepp, A.1    Eckerskorn, C.2    Bogyo, M.3    Baumeister, W.4
  • 33
    • 0036742110 scopus 로고    scopus 로고
    • Compatible solutes of organisms that live in hot saline environments
    • Santos, H., and M. S. da Costa. 2002. Compatible solutes of organisms that live in hot saline environments. Environ. Microbiol. 4:501-509.
    • (2002) Environ. Microbiol. , vol.4 , pp. 501-509
    • Santos, H.1    Da Costa, M.S.2
  • 34
    • 0032211886 scopus 로고    scopus 로고
    • The biosynthesis pathway of di-myo-inositol-1,1′-phosphate in Pyrococcus woesei
    • Scholz, S., S. Wolff, and R. Hensel. 1998. The biosynthesis pathway of di-myo-inositol-1,1′-phosphate in Pyrococcus woesei. FEMS Microbiol. Lett. 168:17-42.
    • (1998) FEMS Microbiol. Lett. , vol.168 , pp. 17-42
    • Scholz, S.1    Wolff, S.2    Hensel, R.3
  • 35
    • 0035212028 scopus 로고    scopus 로고
    • DNA microarray analysis of the hyperthermophilic archaeon Pyrococcus furiosus: Evidence for a new type of sulfur-reducing enzyme complex
    • Schut, G. J., J. Z. Zhou, and M. W. W. Adams. 2001. DNA microarray analysis of the hyperthermophilic archaeon Pyrococcus furiosus: evidence for a new type of sulfur-reducing enzyme complex. J. Bacteriol. 183:7027-7036.
    • (2001) J. Bacteriol. , vol.183 , pp. 7027-7036
    • Schut, G.J.1    Zhou, J.Z.2    Adams, M.W.W.3
  • 36
    • 0032880054 scopus 로고    scopus 로고
    • Expression and heat-responsive regulation of a TFIIB homolog from the archaeon Haloferax volcanii
    • Thompson, D. K., J. R. Palmer, and A. C. J. Daniels. 1999. Expression and heat-responsive regulation of a TFIIB homolog from the archaeon Haloferax volcanii. Mol. Microbiol. 33:1081-1092.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1081-1092
    • Thompson, D.K.1    Palmer, J.R.2    Daniels, A.C.J.3
  • 39
    • 0037414803 scopus 로고    scopus 로고
    • A novel archaeal transcriptional regulator of heat shock response
    • Vierke, G., A. Engelmann, C. Hebbeln, and M. Thomm. 2003. A novel archaeal transcriptional regulator of heat shock response. J. Biol. Chem. 278:18-26.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18-26
    • Vierke, G.1    Engelmann, A.2    Hebbeln, C.3    Thomm, M.4
  • 40
    • 0034520437 scopus 로고    scopus 로고
    • Biochemical systems analysis of genome-wide expression data
    • Voit, E. O., and T. Radivoyevitch. 2000. Biochemical systems analysis of genome-wide expression data. Bioinformatics 16:1023-1037.
    • (2000) Bioinformatics , vol.16 , pp. 1023-1037
    • Voit, E.O.1    Radivoyevitch, T.2
  • 41
    • 0029786325 scopus 로고    scopus 로고
    • Isolation and characterization of the hyperthermostable serine protease, pyrolysin, and its gene from the hyperthermophilic archaeon Pyrococcus furiosus
    • Voorhorst, W. G. B., R. I. L. Eggen, A. C. M. Geerling, C. Platteeuw, R. J. Siezen, and W. M. deVos. 1996. Isolation and characterization of the hyperthermostable serine protease, pyrolysin, and its gene from the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 271:20426-20431.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20426-20431
    • Voorhorst, W.G.B.1    Eggen, R.I.L.2    Geerling, A.C.M.3    Platteeuw, C.4    Siezen, R.J.5    DeVos, W.M.6
  • 42
    • 0034004188 scopus 로고    scopus 로고
    • Purification and characterization of the alanine aminotransferase from the hyperthermophilic archaeon Prococcus furiosus and its role in alanine production
    • Ward, D. E., S. W. M. Kengen, J. van der Oost, and W. M. de Vos. 2000. Purification and characterization of the alanine aminotransferase from the hyperthermophilic archaeon Prococcus furiosus and its role in alanine production. J. Bacteriol. 182:2559-2566.
    • (2000) J. Bacteriol. , vol.182 , pp. 2559-2566
    • Ward, D.E.1    Kengen, S.W.M.2    Van der Oost, J.3    De Vos, W.M.4
  • 44
    • 0029779716 scopus 로고    scopus 로고
    • High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis
    • Xavier, K. B., L. O. Martins, R. Peist, M. Kossmann, W. Boos, and H. Santos. 1996. High-affinity maltose/trehalose transport system in the hyperthermophilic archaeon Thermococcus litoralis. J. Bacteriol. 178:4773-4777.
    • (1996) J. Bacteriol. , vol.178 , pp. 4773-4777
    • Xavier, K.B.1    Martins, L.O.2    Peist, R.3    Kossmann, M.4    Boos, W.5    Santos, H.6


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