메뉴 건너뛰기




Volumn 5, Issue 1, 2010, Pages

Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; GLUCOSE REGULATED PROTEIN 78; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 72; NUCLEOTIDE BINDING PROTEIN; COMPLEMENTARY DNA; ISOPROTEIN;

EID: 77952530199     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0008625     Document Type: Article
Times cited : (118)

References (51)
  • 1
    • 0025100372 scopus 로고
    • 3-Dimensional Structure of the Atpase Fragment of a 70k Heat-Shock Cognate Protein
    • Flaherty KM, DeLuca-Flaherty C, McKay DB (1990) 3-Dimensional Structure of the Atpase Fragment of a 70k Heat-Shock Cognate Protein. Nature 346: 623-628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 2
    • 0031469912 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells
    • Michels AA, Kanon B, Konings AWT, Ohtsuka K, Bensaude O, et al. (1997) Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells. J Biol Chem 272: 33283-33289.
    • (1997) J Biol Chem , vol.272 , pp. 33283-33289
    • Michels, A.A.1    Kanon, B.2    Konings, A.W.T.3    Ohtsuka, K.4    Bensaude, O.5
  • 3
  • 4
    • 0028832266 scopus 로고
    • Characterization of the Nucleotide-Binding Properties and Atpase Activity of Recombinant Hamster Bip Purified from Bacteria
    • Wei JY, Hendershot LM (1995) Characterization of the Nucleotide-Binding Properties and Atpase Activity of Recombinant Hamster Bip Purified from Bacteria. J Biol Chem 270: 26670-26676.
    • (1995) J Biol Chem , vol.270 , pp. 26670-26676
    • Wei, J.Y.1    Hendershot, L.M.2
  • 5
    • 0029037015 scopus 로고
    • Nucleotide-Induced Conformational-Changes in the Atpase and Substrate-Binding Domains of the Dnak Chaperone Provide Evidence for Interdomain Communication
    • Buchberger A, Theyssen H, Schroder H, McCarty JS, Virgallita G, et al. (1995) Nucleotide-Induced Conformational-Changes in the Atpase and Substrate-Binding Domains of the Dnak Chaperone Provide Evidence for Interdomain Communication. J Biol Chem 270: 16903-16910.
    • (1995) J Biol Chem , vol.270 , pp. 16903-16910
    • Buchberger, A.1    Theyssen, H.2    Schroder, H.3    McCarty, J.S.4    Virgallita, G.5
  • 6
    • 0029937037 scopus 로고    scopus 로고
    • Structural analysis of substrate binding by the molecular chaperone DnaK
    • Zhu XT, Zhao X, Burkholder WF, Gragerov A, Ogata CM, et al. (1996) Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272: 1606-1614.
    • (1996) Science , vol.272 , pp. 1606-1614
    • Zhu, X.T.1    Zhao, X.2    Burkholder, W.F.3    Gragerov, A.4    Ogata, C.M.5
  • 7
    • 64649094781 scopus 로고    scopus 로고
    • Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
    • Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ERP (2009) Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc Natl Acad Sci U S A 106: 8471-8476.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 8471-8476
    • Bertelsen, E.B.1    Chang, L.2    Gestwicki, J.E.3    Zuiderweg, E.R.P.4
  • 8
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer MP, Bukau B (2005) Hsp70 chaperones: Cellular functions and molecular mechanism. Cell Mol Life Sci 62: 670-684.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 9
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • Vos MJ, Hageman J, Carra S, Kampinga HH (2008) Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 47: 7001-7011.
    • (2008) Biochemistry , vol.47 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 10
    • 40749101072 scopus 로고    scopus 로고
    • hsp70 genes in the human genome: Conservation and differentiation patterns predict a wide array of overlapping and specialized functions
    • Brocchieri L, de Macario EC, Macario AJL (2008) hsp70 genes in the human genome: Conservation and differentiation patterns predict a wide array of overlapping and specialized functions. BMC Evol Biol 8(19).
    • (2008) BMC Evol Biol , vol.8 , Issue.19
    • Brocchieri, L.1    de Macario, E.C.2    Macario, A.J.L.3
  • 11
    • 49749100105 scopus 로고    scopus 로고
    • Multiple Hsp70 isoforms in the eukaryotic cytosol: Mere redundancy or functional specificity? Curr
    • Kabani M, Martineau CN (2008) Multiple Hsp70 isoforms in the eukaryotic cytosol: Mere redundancy or functional specificity? Curr Genom 9: 338-348.
    • (2008) Genom , vol.9 , pp. 338-348
    • Kabani, M.1    Martineau, C.N.2
  • 12
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
    • Daugaard M, Rohde M, Jaattela M (2007) The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions. FEBS Lett 581: 3702-3710.
    • (2007) FEBS Lett , vol.581 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jaattela, M.3
  • 13
    • 0025095784 scopus 로고
    • Structure and Expression of the 3 Mhc-Linked Hsp70 Genes
    • Milner CM, Campbell RD (1990) Structure and Expression of the 3 Mhc-Linked Hsp70 Genes. Immunogenetics 32: 242-251.
    • (1990) Immunogenetics , vol.32 , pp. 242-251
    • Milner, C.M.1    Campbell, R.D.2
  • 14
    • 0024517766 scopus 로고
    • Human Major Histocompatibility Complex Contains Genes for the Major Heat-Shock Protein-Hsp70
    • Sargent CA, Dunham I, Trowsdale J, Campbell RD (1989) Human Major Histocompatibility Complex Contains Genes for the Major Heat-Shock Protein-Hsp70. Proc Natl Acad Sci U S A 86: 1968-1972.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 1968-1972
    • Sargent, C.A.1    Dunham, I.2    Trowsdale, J.3    Campbell, R.D.4
  • 15
    • 0029060647 scopus 로고
    • Genetic Polymorphisms of the Tnfb and Hsp70 Genes Located in the Human Major Histocompatibility Complex in Sarcoidosis
    • Ishihara M, Ohno S, Ishida T, Mizuki N, Ando H, et al. (1995) Genetic Polymorphisms of the Tnfb and Hsp70 Genes Located in the Human Major Histocompatibility Complex in Sarcoidosis. Tissue Antigens 46: 59-62.
    • (1995) Tissue Antigens , vol.46 , pp. 59-62
    • Ishihara, M.1    Ohno, S.2    Ishida, T.3    Mizuki, N.4    Ando, H.5
  • 16
    • 34548066375 scopus 로고    scopus 로고
    • Association between heat shock protein 70/Hom genetic polymorphisms and uveitis in patients with sarcoidosis
    • Spagnolo P, Sato H, Marshall SE, Antoniou KM, Ahmad T, et al. (2007) Association between heat shock protein 70/Hom genetic polymorphisms and uveitis in patients with sarcoidosis. Inv Ophth Vis Sci 48: 3019-3025.
    • (2007) Inv Ophth Vis Sci , vol.48 , pp. 3019-3025
    • Spagnolo, P.1    Sato, H.2    Marshall, S.E.3    Antoniou, K.M.4    Ahmad, T.5
  • 17
    • 0032697684 scopus 로고    scopus 로고
    • Specific expression of heat shock protein HspA2 in human male germ cells
    • Son WY, Hwang SH, Han CT, Lee JH, Kim S, et al. (1999) Specific expression of heat shock protein HspA2 in human male germ cells. Mol Hum Reprod 5: 1122-1126.
    • (1999) Mol Hum Reprod , vol.5 , pp. 1122-1126
    • Son, W.Y.1    Hwang, S.H.2    Han, C.T.3    Lee, J.H.4    Kim, S.5
  • 18
    • 33845999596 scopus 로고    scopus 로고
    • Post-meiotic shifts in HSPA2/HSP70.2 chaperone activity during mouse spermatogenesis
    • Govin J, Caron C, Escoffier E, Ferro M, Kuhn L, et al. (2006) Post-meiotic shifts in HSPA2/HSP70.2 chaperone activity during mouse spermatogenesis. J Biol Chem 281: 37888-37892.
    • (2006) J Biol Chem , vol.281 , pp. 37888-37892
    • Govin, J.1    Caron, C.2    Escoffier, E.3    Ferro, M.4    Kuhn, L.5
  • 19
    • 0030864750 scopus 로고    scopus 로고
    • HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes
    • Zhu D, Dix DJ, Eddy EM (1997) HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes. Development 124: 3007-3014.
    • (1997) Development , vol.124 , pp. 3007-3014
    • Zhu, D.1    Dix, D.J.2    Eddy, E.M.3
  • 20
    • 0035199033 scopus 로고    scopus 로고
    • Decreased expression of the heat shock protein hsp70-2 is associated with the pathogenesis of male infertility
    • Feng HL, Sandlow JI, Sparks AET (2001) Decreased expression of the heat shock protein hsp70-2 is associated with the pathogenesis of male infertility. Fertil Steril 76: 1136-1139.
    • (2001) Fertil Steril , vol.76 , pp. 1136-1139
    • Feng, H.L.1    Sandlow, J.I.2    Sparks, A.E.T.3
  • 21
    • 49749130037 scopus 로고    scopus 로고
    • Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during spermatogenesis
    • Sasaki T, Marcon E, McQuire T, Arai Y, Moens PB, et al. (2008) Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during spermatogenesis. J Cell Biol 182: 449-458.
    • (2008) J Cell Biol , vol.182 , pp. 449-458
    • Sasaki, T.1    Marcon, E.2    McQuire, T.3    Arai, Y.4    Moens, P.B.5
  • 22
    • 14644435819 scopus 로고    scopus 로고
    • Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
    • Rohde M, Daugaard M, Jensen MH, Helin K, Nylandsted J, et al. (2005) Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev 19: 570-582.
    • (2005) Genes Dev , vol.19 , pp. 570-582
    • Rohde, M.1    Daugaard, M.2    Jensen, M.H.3    Helin, K.4    Nylandsted, J.5
  • 23
    • 0025363926 scopus 로고
    • The Human Heat-Shock Protein Family - Expression of a Novel Heat-Inducible Hsp70 (Hsp70b') and Isolation of Its Cdna and Genomic DNA
    • Leung TKC, Rajendran MY, Monfries C, Hall C, Lim L (1990) The Human Heat-Shock Protein Family - Expression of a Novel Heat-Inducible Hsp70 (Hsp70b') and Isolation of Its Cdna and Genomic DNA. Biochem J 267: 125-132.
    • (1990) Biochem J , vol.267 , pp. 125-132
    • Leung, T.K.C.1    Rajendran, M.Y.2    Monfries, C.3    Hall, C.4    Lim, L.5
  • 24
    • 0026578839 scopus 로고
    • The Human Heat-Shock Genes Hspa6 and Hspa7 Are Both Expressed and Localize to Chromosome-1
    • Leung TKC, Hall C, Rajendran M, Spurr NK, Lim L (1992) The Human Heat-Shock Genes Hspa6 and Hspa7 Are Both Expressed and Localize to Chromosome-1. Genomics 12: 74-79.
    • (1992) Genomics , vol.12 , pp. 74-79
    • Leung, T.K.C.1    Hall, C.2    Rajendran, M.3    Spurr, N.K.4    Lim, L.5
  • 26
    • 0023890443 scopus 로고
    • Human-Gene Encoding the 78,000-Dalton Glucose-Regulated Protein and Its Pseudogene - Structure
    • Ting J, Lee AS (1988) Human-Gene Encoding the 78,000-Dalton Glucose-Regulated Protein and Its Pseudogene - Structure, Conservation, and Regulation. DNA 7: 275-286.
    • (1988) Conservation, and Regulation , vol.DNA 7 , pp. 275-286
    • Ting, J.1    Lee, A.S.2
  • 27
    • 0028198372 scopus 로고
    • Localization of the Gene Encoding Human Bip/Grp78, the Endoplasmic-Reticulum Cognate of the Hsp70 Family, to Chromosome-9q34
    • Hendershot LM, Valentine VA, Lee AS, Morris SW, Shapiro DN (1994) Localization of the Gene Encoding Human Bip/Grp78, the Endoplasmic-Reticulum Cognate of the Hsp70 Family, to Chromosome-9q34. Genomics 20: 281-284.
    • (1994) Genomics , vol.20 , pp. 281-284
    • Hendershot, L.M.1    Valentine, V.A.2    Lee, A.S.3    Morris, S.W.4    Shapiro, D.N.5
  • 28
    • 12344256887 scopus 로고    scopus 로고
    • Building an antibody factory: A job for the unfolded protein response
    • Brewer JW, Hendershot LM (2005) Building an antibody factory: a job for the unfolded protein response. Nature Immunol 6: 23-29.
    • (2005) Nature Immunol , vol.6 , pp. 23-29
    • Brewer, J.W.1    Hendershot, L.M.2
  • 29
    • 34248549003 scopus 로고    scopus 로고
    • GRP78/BiP inhibits endoplasmic reticulum BIK and protects human breast cancer cells against estrogen starvation-induced apoptosis
    • Fu Y, Li JZ, Lee AS (2007) GRP78/BiP inhibits endoplasmic reticulum BIK and protects human breast cancer cells against estrogen starvation-induced apoptosis. Cancer Res 67: 3734-3740.
    • (2007) Cancer Res , vol.67 , pp. 3734-3740
    • Fu, Y.1    Li, J.Z.2    Lee, A.S.3
  • 30
    • 39049160268 scopus 로고    scopus 로고
    • Critical role of the stress chaperone GRP78/BiP in tumor proliferation, survival, and tumor angiogenesis in transgene-induced mammary tumor development
    • Dong DZ, Ni M, Li JZ, Xiong SG, Ye W, et al. (2008) Critical role of the stress chaperone GRP78/BiP in tumor proliferation, survival, and tumor angiogenesis in transgene-induced mammary tumor development. Cancer Res 68: 498-505.
    • (2008) Cancer Res , vol.68 , pp. 498-505
    • Dong, D.Z.1    Ni, M.2    Li, J.Z.3    Xiong, S.G.4    Ye, W.5
  • 31
    • 67649562565 scopus 로고    scopus 로고
    • Functions and pathologies of BiP and its interaction partners
    • Dudek J, Benedix J, Cappel S, Greiner M, Jalal C, et al. (2009) Functions and pathologies of BiP and its interaction partners. Cell Mol Life Sci 66: 1559-1569.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1559-1569
    • Dudek, J.1    Benedix, J.2    Cappel, S.3    Greiner, M.4    Jalal, C.5
  • 32
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
    • Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, et al. (2001) Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291: 1553-1557.
    • (2001) Science , vol.291 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5
  • 33
    • 44649110104 scopus 로고    scopus 로고
    • Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
    • Polier S, Dragovic Z, Hartl FU, Bracher A (2008) Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133: 1068-1079.
    • (2008) Cell , vol.133 , pp. 1068-1079
    • Polier, S.1    Dragovic, Z.2    Hartl, F.U.3    Bracher, A.4
  • 35
    • 57149092290 scopus 로고    scopus 로고
    • Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2
    • Xu Z, Page RC, Gomes MM, Kohli E, Nix JC, et al. (2008) Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2. Nat Struct Mol Biol 15: 1309-1317.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1309-1317
    • Xu, Z.1    Page, R.C.2    Gomes, M.M.3    Kohli, E.4    Nix, J.C.5
  • 36
    • 48149110842 scopus 로고    scopus 로고
    • Exchange we can believe in
    • Hendrickson WA, Liu QL (2008) Exchange we can believe in. Structure 16: 1153-1155.
    • (2008) Structure , vol.16 , pp. 1153-1155
    • Hendrickson, W.A.1    Liu, Q.L.2
  • 37
    • 39549090406 scopus 로고    scopus 로고
    • The use of systematic N- and C-terminal deletions to promote production and structural studies of recombinant proteins
    • Gräslund S, Sagemark J, Berglund H, Dahlgren LG, Flores A, et al. (2008) The use of systematic N- and C-terminal deletions to promote production and structural studies of recombinant proteins. Protein Expr Purif 58: 210-221.
    • (2008) Protein Expr Purif , vol.58 , pp. 210-221
    • Gräslund, S.1    Sagemark, J.2    Berglund, H.3    Dahlgren, L.G.4    Flores, A.5
  • 38
    • 0031569356 scopus 로고    scopus 로고
    • Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain
    • Sriram M, Osipiuk J, Freeman BC, Morimoto RI, Joachimiak A (1997) Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain. Structure 5: 403-414.
    • (1997) Structure , vol.5 , pp. 403-414
    • Sriram, M.1    Osipiuk, J.2    Freeman, B.C.3    Morimoto, R.I.4    Joachimiak, A.5
  • 40
    • 20844448232 scopus 로고    scopus 로고
    • A comprehensive and non-redundant database of protein domain movements
    • Qi G, Lee R, Hayward S (2005) A comprehensive and non-redundant database of protein domain movements. Bioinformatics 21: 2832-2838.
    • (2005) Bioinformatics , vol.21 , pp. 2832-2838
    • Qi, G.1    Lee, R.2    Hayward, S.3
  • 42
    • 1642464581 scopus 로고    scopus 로고
    • The second metal-binding site of 70 kDa heat-shock protein is essential for ADP binding, ATP hydrolysis and ATP synthesis
    • Wu X, Yano M, Washida H, Kido H (2004) The second metal-binding site of 70 kDa heat-shock protein is essential for ADP binding, ATP hydrolysis and ATP synthesis. Biochem J 378: 793-799.
    • (2004) Biochem J , vol.378 , pp. 793-799
    • Wu, X.1    Yano, M.2    Washida, H.3    Kido, H.4
  • 43
    • 0026076490 scopus 로고
    • DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity
    • McCarty JS, Walker GC (1991) DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc Natl Acad Sci U S A 88: 9513-9517.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 9513-9517
    • McCarty, J.S.1    Walker, G.C.2
  • 44
    • 0027194027 scopus 로고
    • The immunoglobulin-binding protein in vitro autophosphorylation site maps to a threonine within the ATP binding cleft but is not a detectable site of in vivo phosphorylation
    • Gaut JR, Hendershot LM (1993) The immunoglobulin-binding protein in vitro autophosphorylation site maps to a threonine within the ATP binding cleft but is not a detectable site of in vivo phosphorylation. J Biol Chem 268: 12691-12698.
    • (1993) J Biol Chem , vol.268 , pp. 12691-12698
    • Gaut, J.R.1    Hendershot, L.M.2
  • 45
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26: 795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 46
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P (2006) Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62: 72-82.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 47
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin A, Teplyakov A (2000) An approach to multi-copy search in molecular replacement. Acta Crystallogr D Biol Crystallogr 56: 1622-1624.
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 49
  • 50
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis IW, Murray LW, Richardson JS, Richardson DC (2004) MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res 32: W615-W619.
    • (2004) Nucleic Acids Res , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 51
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15: 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.