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Volumn 36, Issue 1, 2009, Pages 127-134

Molecular cloning and expression analysis of a heat shock protein (Hsp90) gene from black tiger shrimp (Penaeus monodon)

Author keywords

Black tiger shrimp (Penaeus monodon); Cloning; Hsp90; RT expression

Indexed keywords

AMINO ACID; HEAT SHOCK PROTEIN 90; POLYPEPTIDE;

EID: 56649085109     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-007-9160-9     Document Type: Article
Times cited : (55)

References (43)
  • 2
    • 0028047925 scopus 로고
    • Genetic evidence for a common pathway mediating dative stress, inflammatory gene induction, and aortic fatty streak formation in mice
    • F Liao A Andalibi JH Qiao H Allayee AM Fogelman AJ Lusis 1994 Genetic evidence for a common pathway mediating dative stress, inflammatory gene induction, and aortic fatty streak formation in mice J Clin Invest 94 877 884
    • (1994) J Clin Invest , vol.94 , pp. 877-884
    • Liao, F.1    Andalibi, A.2    Qiao, J.H.3    Allayee, H.4    Fogelman, A.M.5    Lusis, A.J.6
  • 4
    • 0028916211 scopus 로고
    • Heat shock proteins and protection against myocardial ischemia
    • R Mestril WH Dillmann 1995 Heat shock proteins and protection against myocardial ischemia J Mol Cell Cardiol 27 45 52
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 45-52
    • Mestril, R.1    Dillmann, W.H.2
  • 5
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 and Co.-a holding for folding
    • J Buchner 1999 hsp90 and Co.-a holding for folding Trends Biochem Sci 24 136 141
    • (1999) Trends Biochem Sci , vol.24 , pp. 136-141
    • Buchner, J.1
  • 6
    • 0028061311 scopus 로고
    • Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
    • EA Craig JS Weissman AL Horwich 1994 Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell Cell 78 365 372
    • (1994) Cell , vol.78 , pp. 365-372
    • Craig, E.A.1    Weissman, J.S.2    Horwich, A.L.3
  • 7
    • 0028044818 scopus 로고
    • Balance of expression of genes coding for extracellular matrix proteins and extracellular matrix degrading proteases in chronic pancreatitis
    • TM Gress F Muller-Pillasch C Weber MM Lerch H Freiss M Buchler HG Beger G Adler 1994 Balance of expression of genes coding for extracellular matrix proteins and extracellular matrix degrading proteases in chronic pancreatitis Cancer Res 54 547 551
    • (1994) Cancer Res , vol.54 , pp. 547-551
    • Gress, T.M.1    Muller-Pillasch, F.2    Weber, C.3    Lerch, M.M.4    Freiss, H.5    Buchler, M.6    Beger, H.G.7    Adler, G.8
  • 8
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • L Whitesell EG Mimnaugh B De Costa CE Myers LM Neckers 1994 Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation Proc Natl Acad Sci USA 91 8324 8328
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 9
    • 0028589101 scopus 로고
    • A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90
    • R Aligue H Akhavan-Niak P Russell 1994 A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90 EMBO J 13 6099 6106
    • (1994) EMBO J , vol.13 , pp. 6099-6106
    • Aligue, R.1    Akhavan-Niak, H.2    Russell, P.3
  • 10
    • 0028366212 scopus 로고
    • Heat shock proteins transfer peptides during antigen processing and CTL priming
    • PK Srivastava H Udono NE Blachere Z Li 1994 Heat shock proteins transfer peptides during antigen processing and CTL priming Immunogenetics 39 93 98
    • (1994) Immunogenetics , vol.39 , pp. 93-98
    • Srivastava, P.K.1    Udono, H.2    Blachere, N.E.3    Li, Z.4
  • 11
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of HSP90 and small HSPs as molecular chaperones
    • U Jakob J Buchner 1994 Assisting spontaneity: the role of HSP90 and small HSPs as molecular chaperones Trends Biochem Sci 19 205 211
    • (1994) Trends Biochem Sci , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 12
    • 0027447541 scopus 로고
    • Steroid receptors and their associated proteins
    • DF Smith DO Toft 1993 Steroid receptors and their associated proteins Mol Endocrinol 7 4 11
    • (1993) Mol Endocrinol , vol.7 , pp. 4-11
    • Smith, D.F.1    Toft, D.O.2
  • 13
    • 0030808079 scopus 로고    scopus 로고
    • Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus
    • MJ Czar MJ Welsh WB Pratt 1997 Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus J Biochem 36 7776 7785
    • (1997) J Biochem , vol.36 , pp. 7776-7785
    • Czar, M.J.1    Welsh, M.J.2    Pratt, W.B.3
  • 14
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system
    • LF Stancato YH Chow KA Hutchison GH Perdew R Jove WB Pratt 1993 Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system J Biochem 268 21711 21716
    • (1993) J Biochem , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.H.2    Hutchison, K.A.3    Perdew, G.H.4    Jove, R.5    Pratt, W.B.6
  • 15
    • 0022342203 scopus 로고
    • Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein
    • FR Sanchez DO Toft MJ Schlesinger WB Pratt 1985 Evidence that the 90-kDa phosphoprotein associated with the untransformed L-cell glucocorticoid receptor is a murine heat shock protein J Biochem 260 12398 13401
    • (1985) J Biochem , vol.260 , pp. 12398-13401
    • Sanchez, F.R.1    Toft, D.O.2    Schlesinger, M.J.3    Pratt, W.B.4
  • 16
    • 0029844672 scopus 로고    scopus 로고
    • Immunofluorescence localization of the 90-kDa heat-shock protein to cytoskeleton
    • MJ Czar MD Galigniana AM Silverstein WB Pratt 1996 Immunofluorescence localization of the 90-kDa heat-shock protein to cytoskeleton Eur J Cell Biol 70 322 330
    • (1996) Eur J Cell Biol , vol.70 , pp. 322-330
    • Czar, M.J.1    Galigniana, M.D.2    Silverstein, A.M.3    Pratt, W.B.4
  • 17
    • 0025874261 scopus 로고
    • Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90
    • Y Minami H Kawasaki Y Miyata K Suzuki I Yahara 1991 Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90 J Biochem 266 10099 10103
    • (1991) J Biochem , vol.266 , pp. 10099-10103
    • Minami, Y.1    Kawasaki, H.2    Miyata, Y.3    Suzuki, K.4    Yahara, I.5
  • 18
    • 0028181755 scopus 로고
    • Association of the beta gamma subunits of trimeric GTP-binding proteins with 90-kDa heat shock protein, hsp90
    • A Inanobe K Takahashi T Katada 1994 Association of the beta gamma subunits of trimeric GTP-binding proteins with 90-kDa heat shock protein, hsp90 J Biochem 115 486 492
    • (1994) J Biochem , vol.115 , pp. 486-492
    • Inanobe, A.1    Takahashi, K.2    Katada, T.3
  • 19
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. a comprehensive review
    • P Csermely T Schnaider C Soti Z Prohászka G Nardai 1998 The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review Pharmacol Ther 79 129 168
    • (1998) Pharmacol Ther , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohászka, Z.4    Nardai, G.5
  • 20
    • 0033621681 scopus 로고    scopus 로고
    • Mice lacking hsp90_fail to develop a placental labyrinth
    • AL Voss T Thomas P Gruss 2000 Mice lacking hsp90_fail to develop a placental labyrinth Development 127 1 11
    • (2000) Development , vol.127 , pp. 1-11
    • Voss, A.L.1    Thomas, T.2    Gruss, P.3
  • 21
    • 0028276119 scopus 로고
    • How the cell copes with stress and the function of heat shock proteins
    • MJ Schlesinger 1994 How the cell copes with stress and the function of heat shock proteins Pediatr Res 36 1 6
    • (1994) Pediatr Res , vol.36 , pp. 1-6
    • Schlesinger, M.J.1
  • 22
    • 0029188297 scopus 로고
    • Heat-shock proteins and molecular chaperones; Implications for pathogenesis, diagnostics, and therapeutics
    • AJL Macario 1995 Heat-shock proteins and molecular chaperones; implications for pathogenesis, diagnostics, and therapeutics Int J Clin Lab Res 25 59 70
    • (1995) Int J Clin Lab Res , vol.25 , pp. 59-70
    • MacArio, A.J.L.1
  • 23
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • C Georgopoulos WJ Welch 1993 Role of the major heat shock proteins as molecular chaperones Annu Rev Cell Biol 9 601 634
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 24
    • 33750514804 scopus 로고    scopus 로고
    • Discovery of the genes in response to white spot syndrome virus (WSSV) infection in Fenneropenaeus chinensis through cDNA microarray
    • B Wang F-h Li B Dong X-j Zhang C-s Zhang J-h Xiang 2006 Discovery of the genes in response to white spot syndrome virus (WSSV) infection in Fenneropenaeus chinensis through cDNA microarray Mar Biotechnol 8 491 500
    • (2006) Mar Biotechnol , vol.8 , pp. 491-500
    • Wang, B.1    Li, F.-H.2    Dong, B.3    Zhang, X.-J.4    Zhang, C.-S.5    Xiang, J.-H.6
  • 25
    • 48249140138 scopus 로고    scopus 로고
    • Morphological and histological observation on ovary development of Penaeus monodon from northern South China Sea
    • 3
    • JH Huang FL Zhou ZM Ma SG Jiang 2005 Morphological and histological observation on ovary development of Penaeus monodon from northern South China Sea J Trop Oceanogr 25 3 47 52
    • (2005) J Trop Oceanogr , vol.25 , pp. 47-52
    • Huang, J.H.1    Zhou, F.L.2    Ma, Z.M.3    Jiang, S.G.4
  • 26
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTALX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • JD Thompson TJ Gibson F Plewniak F Jeanmougin DG Higgins 1997 The CLUSTALX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res 25 4876 4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 27
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • S Kumar K Tamura M Nei 2004 MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment Brief Bioinform 5 150 163
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 28
    • 0038185346 scopus 로고    scopus 로고
    • Posttranscriptional regulation of gene expression by degradation of messenger RNAs
    • A Bevilacqua MC Ceriani S Capaccioli A Nicolin 2003 Posttranscriptional regulation of gene expression by degradation of messenger RNAs J Cell Physiol 195 356 372
    • (2003) J Cell Physiol , vol.195 , pp. 356-372
    • Bevilacqua, A.1    Ceriani, M.C.2    Capaccioli, S.3    Nicolin, A.4
  • 29
    • 0036864153 scopus 로고    scopus 로고
    • AU-rich element mediated translational control: Complexity and multiple activities of trans-activating factors
    • T Zhang V Kruys G Huez C Gueydan 2002 AU-rich element mediated translational control: complexity and multiple activities of trans-activating factors Biochem Soc Trans 30 952 958
    • (2002) Biochem Soc Trans , vol.30 , pp. 952-958
    • Zhang, T.1    Kruys, V.2    Huez, G.3    Gueydan, C.4
  • 30
    • 0346725103 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two different cDNAs encoding the molecular chaperone Hsp90 in the Oomycete Achlya ambisexualis
    • SA Brunt JC Silver 2004 Molecular cloning and characterization of two different cDNAs encoding the molecular chaperone Hsp90 in the Oomycete Achlya ambisexualis Fungal Genet Biol 41 239 252
    • (2004) Fungal Genet Biol , vol.41 , pp. 239-252
    • Brunt, S.A.1    Silver, J.C.2
  • 31
    • 0023224123 scopus 로고
    • Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family
    • NF Rebbe J Ware RM Bertina P Modrich DW Stafford 1987 Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family Gene 53 235 245
    • (1987) Gene , vol.53 , pp. 235-245
    • Rebbe, N.F.1    Ware, J.2    Bertina, R.M.3    Modrich, P.4    Stafford, D.W.5
  • 32
    • 0024364170 scopus 로고
    • Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein
    • E Hickey SE Brandon G Smale D Lloyd LA Weber 1989 Sequence and regulation of a gene encoding a human 89-kilodalton heat shock protein Mol Cell Biol 9 2615 2626
    • (1989) Mol Cell Biol , vol.9 , pp. 2615-2626
    • Hickey, E.1    Brandon, S.E.2    Smale, G.3    Lloyd, D.4    Weber, L.A.5
  • 33
    • 0031826869 scopus 로고    scopus 로고
    • Searching DNA databases for similarities to DNA sequences: When is a match significant?
    • 4
    • I Anderson A Brass 1998 Searching DNA databases for similarities to DNA sequences: when is a match significant? Bioinformatics 14 4 349
    • (1998) Bioinformatics , vol.14 , pp. 349
    • Anderson, I.1    Brass, A.2
  • 34
    • 0024357643 scopus 로고
    • The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat shock protein, hsp90 alpha at two NH2-terminal threonine residues
    • SP Lees-Miller CW Anderson 1989 The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat shock protein, hsp90 alpha at two NH2-terminal threonine residues J Biochem 264 17275 17280
    • (1989) J Biochem , vol.264 , pp. 17275-17280
    • Lees-Miller, S.P.1    Anderson, C.W.2
  • 35
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • DK Eggers WJ Welch WJ Hansen 1997 Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells Mol Biol Cell 8 1559 1573
    • (1997) Mol Biol Cell , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 36
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • C Prodromou SM Roe R O'Brien JE Ladbury PW Piper LH Pearl 1997 Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone Cell 90 65 75
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 37
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • CE Stebbins AA Russo C Schneider N Rosen FU Hartl NP Pavletich 1997 Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent Cell 89 239 250
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 39
    • 0242661627 scopus 로고    scopus 로고
    • Molecular cloning of the 82-kDa heat shock protein (HSP90) of Toxoplasma gondii associated with the entry into and growth in host cells
    • HJ Ahn S Kim HW Nam 2003 Molecular cloning of the 82-kDa heat shock protein (HSP90) of Toxoplasma gondii associated with the entry into and growth in host cells Biochem Biophys Res Commun 311 654 659
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 654-659
    • Ahn, H.J.1    Kim, S.2    Nam, H.W.3
  • 40
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
    • DF Nathan MH Vos S Lindquist 1997 In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone Proc Natl Acad Sci USA 94 12949 12956
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 41
    • 0029120998 scopus 로고
    • Expression of heat shock protein 90 (hsp90) in neural and nonneural tissues of the control and hyperthermic rabbit
    • H Quraishi IR Brown 1995 Expression of heat shock protein 90 (hsp90) in neural and nonneural tissues of the control and hyperthermic rabbit Exp Cell Res 219 358 363
    • (1995) Exp Cell Res , vol.219 , pp. 358-363
    • Quraishi, H.1    Brown, I.R.2
  • 42
    • 52649104423 scopus 로고    scopus 로고
    • Perification and characterization of porcine testis 90-kDa heat shock protein (Hsp90) as a substrate for various protein kinases
    • HC Huang JS Yu CC Tsay JH Lin SY Huang WT Fang YC Liu BS Tzang WC Lee 2002 Perification and characterization of porcine testis 90-kDa heat shock protein (Hsp90) as a substrate for various protein kinases J Protein Chem 21 111 121
    • (2002) J Protein Chem , vol.21 , pp. 111-121
    • Huang, H.C.1    Yu, J.S.2    Tsay, C.C.3    Lin, J.H.4    Huang, S.Y.5    Fang, W.T.6    Liu, Y.C.7    Tzang, B.S.8    Lee, W.C.9
  • 43
    • 0033590623 scopus 로고    scopus 로고
    • Molecular cloning and characterization of porcine cDNA encoding a 90-kDa heat shock protein and its expression following hyperthermia
    • H-c Huang W-c Lee J-h Lin H-w Huang S-c Jian SJT Mao P-c Yang T-y Huang Y-c Liu 1999 Molecular cloning and characterization of porcine cDNA encoding a 90-kDa heat shock protein and its expression following hyperthermia Gene 226 307 315
    • (1999) Gene , vol.226 , pp. 307-315
    • Huang, H.-C.1    Lee, W.-C.2    Lin, J.-H.3    Huang, H.-W.4    Jian, S.-C.5    Mao, S.J.T.6    Yang, P.-C.7    Huang, T.-Y.8    Liu, Y.-C.9


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