메뉴 건너뛰기




Volumn 16, Issue 1, 2004, Pages 23-28

The gene for the heat-shock protein 70 of Euplotes focardii, an Antarctic psychrophilic ciliate

Author keywords

Antarctic biology; Cold adaptation; HSE and StRE cis acting elements; Protozoa; Stress inducible genes

Indexed keywords

HEAT SHOCK;

EID: 1542378751     PISSN: 09541020     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0954102004001774     Document Type: Conference Paper
Times cited : (28)

References (32)
  • 1
    • 0037424811 scopus 로고    scopus 로고
    • Structural characterization of En-1, a cold adapted protein pheromone isolated from the Antarctic ciliate Euplotes nobilii
    • ALIMENTI, C., ORTENZI, C., CARRATORE, V. & LUPORINI, P. 2003. Structural characterization of En-1, a cold adapted protein pheromone isolated from the Antarctic ciliate Euplotes nobilii. Biochimica et Biophysica Acta, 1621, 17-21.
    • (2003) Biochimica et Biophysica Acta , vol.1621 , pp. 17-21
    • Alimenti, C.1    Ortenzi, C.2    Carratore, V.3    Luporini, P.4
  • 2
    • 0030033995 scopus 로고    scopus 로고
    • A gene-sized DNA molecule encoding heat-shock protein 70 in Oxytricha nova
    • ANDERSON, R.C., LINDAUER, K.R. & PRESCOTT, D.M. 1996. A gene-sized DNA molecule encoding heat-shock protein 70 in Oxytricha nova. Gene, 168, 103-107.
    • (1996) Gene , vol.168 , pp. 103-107
    • Anderson, R.C.1    Lindauer, K.R.2    Prescott, D.M.3
  • 4
    • 0032134221 scopus 로고    scopus 로고
    • The lack of a stress response in Hydra oligactis is due to reduced Hsp70 mRNA stability
    • BRENNECKE, T., GELLER, K. & BOSCH, T.C.G. 1998. The lack of a stress response in Hydra oligactis is due to reduced Hsp70 mRNA stability. European Journal of Biochemistry, 255, 703-709.
    • (1998) European Journal of Biochemistry , vol.255 , pp. 703-709
    • Brennecke, T.1    Geller, K.2    Bosch, T.C.G.3
  • 5
    • 2642689664 scopus 로고    scopus 로고
    • The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors
    • DEMAND, J., LUDERS, J. & HOHFELD, J. 1998. The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Molecular and Cellular Biology, 18, 2023-2028.
    • (1998) Molecular and Cellular Biology , vol.18 , pp. 2023-2028
    • Demand, J.1    Luders, J.2    Hohfeld, J.3
  • 7
    • 0033813390 scopus 로고    scopus 로고
    • Stress-controlled transcription factors, stress-induced genes and stress tolerance in budding yeast
    • ESTRUCH, F. 2000. Stress-controlled transcription factors, stress-induced genes and stress tolerance in budding yeast. FEMS Microbiology Review, 24, 469-486.
    • (2000) FEMS Microbiology Review , vol.24 , pp. 469-486
    • Estruch, F.1
  • 8
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response: Evolutionary and ecological physiology
    • FEDER, M.E. & HOFMANN, G.E. 1999. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annual Review of Physiology, 61, 243-282.
    • (1999) Annual Review of Physiology , vol.61 , pp. 243-282
    • Feder, M.E.1    Hofmann, G.E.2
  • 9
    • 0021381028 scopus 로고
    • A technique for radiolabelling restriction endonuclease fragments to high specific activity
    • FEINBERG, A.P. & VOGELSTEIN, B. 1984. A technique for radiolabelling restriction endonuclease fragments to high specific activity. Analytical Biochemistry, 137, 266-267.
    • (1984) Analytical Biochemistry , vol.137 , pp. 266-267
    • Feinberg, A.P.1    Vogelstein, B.2
  • 10
    • 0002616870 scopus 로고
    • Structure and regulation of heat-shock gene promoters
    • Morimoto, R., Tissières, A. & Georgopoulos, C., eds. New York, NY: Cold Spring Harbor Laboratory Press
    • FERNANDES, M., O'BRIEN, T. & LIS, J.T. 1994. Structure and regulation of heat-shock gene promoters. In MORIMOTO, R., TISSIÈRES, A. & GEORGOPOULOS, C., eds. The biology of heat-shock proteins and molecular chaperones. New York, NY: Cold Spring Harbor Laboratory Press, 375-394.
    • (1994) The Biology of Heat-shock Proteins and Molecular Chaperones , pp. 375-394
    • Fernandes, M.1    O'Brien, T.2    Lis, J.T.3
  • 11
    • 0032530086 scopus 로고    scopus 로고
    • Hot spots in cold adaptation: Localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes
    • FIELDS, P.A. & SOMERO, G.N. 1998. Hot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishes. Proceedings of the National Academy of Sciences of the United States of America, 95, 11476-11481.
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , pp. 11476-11481
    • Fields, P.A.1    Somero, G.N.2
  • 12
    • 0027051403 scopus 로고
    • Cloning and expression of a heat-inducible Hsp70 gene in two species of Hydra which differ in their stress response
    • GELLER, K., PRAETZEL, G. & BOSCH, T.C.G. 1992. Cloning and expression of a heat-inducible Hsp70 gene in two species of Hydra which differ in their stress response. European Journal of Biochemistry, 210, 683-691.
    • (1992) European Journal of Biochemistry , vol.210 , pp. 683-691
    • Geller, K.1    Praetzel, G.2    Bosch, T.C.G.3
  • 13
    • 0028300548 scopus 로고
    • Characterization of transcription initiation, translation initiation, and poly(A) addition sites in the gene-sized macronuclear DNA molecules of Euplotes
    • GHOSH, S., JARACZEWSKI, J.W., KLOBUTCHER, L.A. & JAHN, C.L. 1994. Characterization of transcription initiation, translation initiation, and poly(A) addition sites in the gene-sized macronuclear DNA molecules of Euplotes. Nucleic Acids Research, 22, 214-221.
    • (1994) Nucleic Acids Research , vol.22 , pp. 214-221
    • Ghosh, S.1    Jaraczewski, J.W.2    Klobutcher, L.A.3    Jahn, C.L.4
  • 14
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-Model and the Swiss-PdbViewer: An environment for comparative protein modelling
    • GUEX, N. & PEITSCH, M.C. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 15
    • 0033836161 scopus 로고    scopus 로고
    • Heat-shock protein expression is absent in the Antarctic fish Trematomus bernacchii (family Nototheniidae)
    • HOFMANN, G.E., BRADLEY, A.B., AIRAKSINEN, S., KEEN, J.E. & SOMERO, GN. 2000. Heat-shock protein expression is absent in the Antarctic fish Trematomus bernacchii (family Nototheniidae). Journal of Experimental Biology, 203, 2331-2339.
    • (2000) Journal of Experimental Biology , vol.203 , pp. 2331-2339
    • Hofmann, G.E.1    Bradley, A.B.2    Airaksinen, S.3    Keen, J.E.4    Somero, G.N.5
  • 16
    • 0027441585 scopus 로고
    • Identification of cis and trans components of a novel heat-shock stress regulatory pathway in Saccharomyces cerevisiae
    • KOBAYASHI, N. & MCENTEE, K. 1993. Identification of cis and trans components of a novel heat-shock stress regulatory pathway in Saccharomyces cerevisiae. Molecular and Cellular Biology, 13, 248-256.
    • (1993) Molecular and Cellular Biology , vol.13 , pp. 248-256
    • Kobayashi, N.1    McEntee, K.2
  • 17
    • 0035052289 scopus 로고    scopus 로고
    • Divergence between two Antarctic species of the ciliate Euplotes, E. focardii and E. nobilii, in the expression of heat-shock protein 70 genes
    • LA TERZA, A., PAPA, G., MICELI, C. & LUPORINI, P. 2001. Divergence between two Antarctic species of the ciliate Euplotes, E. focardii and E. nobilii, in the expression of heat-shock protein 70 genes. Molecular Ecology, 10, 1061-1067.
    • (2001) Molecular Ecology , vol.10 , pp. 1061-1067
    • La Terza, A.1    Papa, G.2    Miceli, C.3    Luporini, P.4
  • 18
    • 0033603631 scopus 로고    scopus 로고
    • High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70
    • MORSHAUSER, R.C., HU, W., WANG, H., PANG, Y., FLYNN, G.C. & ZUIDERWEG, E.R. 1999. High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70. Journal of Molecular Biology, 289, 1387-403.
    • (1999) Journal of Molecular Biology , vol.289 , pp. 1387-1403
    • Morshauser, R.C.1    Hu, W.2    Wang, H.3    Pang, Y.4    Flynn, G.C.5    Zuiderweg, E.R.6
  • 19
    • 0002692725 scopus 로고
    • Taxonomy and ecology of ciliate fauna (Protozoa, Ciliophora) in the endopelagial and pelagial of the Weddell Sea, Antarctica
    • PETZ, W., SONG, W. & WILBERT, N. 1995. Taxonomy and ecology of ciliate fauna (Protozoa, Ciliophora) in the endopelagial and pelagial of the Weddell Sea, Antarctica. Stapfia, 40, 1-223.
    • (1995) Stapfia , vol.40 , pp. 1-223
    • Petz, W.1    Song, W.2    Wilbert, N.3
  • 20
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat-shock transcription factors in regulation of the heat-shock response and beyond
    • PIRKKALA, L., NYKANEN, P. & SISTONEN, L. 2001. Roles of the heat-shock transcription factors in regulation of the heat-shock response and beyond. FASEB Journal, 15, 1118-1131.
    • (2001) FASEB Journal , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykanen, P.2    Sistonen, L.3
  • 21
    • 0030772842 scopus 로고    scopus 로고
    • Cold-adapted microtubules: Characterization of tubulin posttranslational modifications in the Antarctic ciliate Euplotes focardii
    • PUCCIARELLI, S., BALLARINI, P. & MICELI, C. 1997. Cold-adapted microtubules: characterization of tubulin posttranslational modifications in the Antarctic ciliate Euplotes focardii. Cell Molility and the Cytoskeleton, 38, 329-340.
    • (1997) Cell Molility and the Cytoskeleton , vol.38 , pp. 329-340
    • Pucciarelli, S.1    Ballarini, P.2    Miceli, C.3
  • 22
    • 0036783049 scopus 로고    scopus 로고
    • Characterization of the cold-adapted alpha-tubulin from the psychrophilic ciliate Euplotes focardii
    • PUCCIARELLI, S. & MICELI, C. 2002. Characterization of the cold-adapted alpha-tubulin from the psychrophilic ciliate Euplotes focardii. Extremophiles, 6, 385-389.
    • (2002) Extremophiles , vol.6 , pp. 385-389
    • Pucciarelli, S.1    Miceli, C.2
  • 23
    • 0036451228 scopus 로고    scopus 로고
    • Heterologous expression and folding analysis of a beta-tubulin isotype from the Antarctic ciliate Euplotes focardii
    • PUCCIARELLI, S., MICELI, C. & MELKI, R. 2002. Heterologous expression and folding analysis of a beta-tubulin isotype from the Antarctic ciliate Euplotes focardii. European Journal of Biochemistry, 269, 6271-6277.
    • (2002) European Journal of Biochemistry , vol.269 , pp. 6271-6277
    • Pucciarelli, S.1    Miceli, C.2    Melki, R.3
  • 24
    • 0029395010 scopus 로고
    • Stress signalling in yeast
    • RUIS, H. & SCHULLER, C. 1995. Stress signalling in yeast. Bioessays, 17, 959-965.
    • (1995) Bioessays , vol.17 , pp. 959-965
    • Ruis, H.1    Schuller, C.2
  • 26
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • SCHEUFLER, C., BRINKER, A., BOURENKOV, G., PEGORARO, S., MORODER, L., BARTUNIK, H., HARTL, F.U. & MOAREFI, I. 2000. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell, 101, 199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 27
    • 0030003064 scopus 로고    scopus 로고
    • Msn2p, a zinc finger DNA-binding protein, is the transcriptional activator of the multistress response in Saccharomyces cerevisiae
    • SCHMITT, A.P. & MCENTEE, K. 1996. Msn2p, a zinc finger DNA-binding protein, is the transcriptional activator of the multistress response in Saccharomyces cerevisiae. Proceedings of the National Academy of Sciences of the United States of America, 93, 5777-5782.
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , pp. 5777-5782
    • Schmitt, A.P.1    Mcentee, K.2
  • 29
    • 0031569356 scopus 로고    scopus 로고
    • Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain
    • SRIRAM, M., OSIPIUK, J., FREEMAN, B., MORIMOTO, R. & JOACHIMIAK, A. 1997. Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain. Structure, 5, 403-14.
    • (1997) Structure , vol.5 , pp. 403-414
    • Sriram, M.1    Osipiuk, J.2    Freeman, B.3    Morimoto, R.4    Joachimiak, A.5
  • 30
    • 0002754168 scopus 로고
    • Description of two new species of Euplotes and Euplotes rariseta from Antarctica
    • VALBONESI, A. & LUPORINI, P. 1990. Description of two new species of Euplotes and Euplotes rariseta from Antarctica. Polar Biology, 11, 47-53.
    • (1990) Polar Biology , vol.11 , pp. 47-53
    • Valbonesi, A.1    Luporini, P.2
  • 31
    • 0027844168 scopus 로고
    • Biology of Euplotes focardii, an Antarctic ciliate
    • VALBONESI, A. & LUPORINI, P. 1993. Biology of Euplotes focardii, an Antarctic ciliate. Polar Biology, 13, 489-493.
    • (1993) Polar Biology , vol.13 , pp. 489-493
    • Valbonesi, A.1    Luporini, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.