메뉴 건너뛰기




Volumn 156, Issue , 2006, Pages 1-21

The diverse roles of J-proteins, the obligate Hsp70 co-chaperone

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 70;

EID: 33646847503     PISSN: 03034240     EISSN: None     Source Type: Book Series    
DOI: 10.1007/s10254-005-0001-8     Document Type: Review
Times cited : (185)

References (104)
  • 1
    • 18844400606 scopus 로고    scopus 로고
    • In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae
    • Aron R, Lopez N, Walter W, Craig EA, Johnson J (2005) In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae. Genetics 169:1873-1882
    • (2005) Genetics , vol.169 , pp. 1873-1882
    • Aron, R.1    Lopez, N.2    Walter, W.3    Craig, E.A.4    Johnson, J.5
  • 2
    • 0029954823 scopus 로고    scopus 로고
    • Functional interaction of cytosolic Hsp70 and DnaJ-related protein, Ydj1p, in protein translocation in vivo
    • Becker J, Walter W, Yan W, Craig EA (1996) Functional interaction of cytosolic Hsp70 and DnaJ-related protein, Ydj1p, in protein translocation in vivo. Mol Cell Biol 16:4378-4386
    • (1996) Mol Cell Biol , vol.16 , pp. 4378-4386
    • Becker, J.1    Walter, W.2    Yan, W.3    Craig, E.A.4
  • 3
    • 0037424360 scopus 로고    scopus 로고
    • Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae
    • Beilharz T, Egan B, Silver PA, Hofmann K, Lithgow T (2003) Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae. J Biol Chem 278:8219-8223
    • (2003) J Biol Chem , vol.278 , pp. 8219-8223
    • Beilharz, T.1    Egan, B.2    Silver, P.A.3    Hofmann, K.4    Lithgow, T.5
  • 4
    • 0034680778 scopus 로고    scopus 로고
    • Berjanskii MV, Riley MI, Xie A, Semenchenko V, Folk WR, Van Doren SR (2000) NMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigens. J Biol Chem 275:36094-36103
    • Berjanskii MV, Riley MI, Xie A, Semenchenko V, Folk WR, Van Doren SR (2000) NMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigens. J Biol Chem 275:36094-36103
  • 5
    • 17144371281 scopus 로고    scopus 로고
    • Low resolution structural study of two human HSP40 chaperones in solution. DJA1 from subfamily A and DJB4 from subfamily B have different quaternary structures
    • Borges JC, Fischer H, Craievich AF, Ramos CH (2005) Low resolution structural study of two human HSP40 chaperones in solution. DJA1 from subfamily A and DJB4 from subfamily B have different quaternary structures. J Biol Chem 280:13671-13681
    • (2005) J Biol Chem , vol.280 , pp. 13671-13681
    • Borges, J.C.1    Fischer, H.2    Craievich, A.F.3    Ramos, C.H.4
  • 6
    • 0021471706 scopus 로고
    • Dissociation of clathrin coats coupled to the hydrolysis of ATP: Role of an uncoating ATPase
    • Braell W, Schlossman D, Schmid S, Rothmann J (1984) Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase. J Cell Biol 99:734-741
    • (1984) J Cell Biol , vol.99 , pp. 734-741
    • Braell, W.1    Schlossman, D.2    Schmid, S.3    Rothmann, J.4
  • 7
    • 10344253818 scopus 로고    scopus 로고
    • Cell biology: Clathrin's Achilles' ankle
    • Brodsky FM (2004) Cell biology: clathrin's Achilles' ankle. Nature 432:568-569
    • (2004) Nature , vol.432 , pp. 568-569
    • Brodsky, F.M.1
  • 8
    • 22444438841 scopus 로고    scopus 로고
    • Ribosomes catch Hsp70s
    • Bukau B (2005) Ribosomes catch Hsp70s. Nat Struct Mol Biol 12:472-473
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 472-473
    • Bukau, B.1
  • 9
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92:351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 10
    • 0025745326 scopus 로고
    • Characterization of YDJ1: A yeast homologue of the bacterial dnaJ protein
    • Caplan AJ, Douglas MG (1991) Characterization of YDJ1: A yeast homologue of the bacterial dnaJ protein. J Cell Biol 114:609-621
    • (1991) J Cell Biol , vol.114 , pp. 609-621
    • Caplan, A.J.1    Douglas, M.G.2
  • 11
    • 0026686468 scopus 로고
    • Farnesylation of YDJ1p is required for function at elevated growth temperatures in S. cerevisiae
    • Caplan AJ, Tsai J, Casey PJ, Douglas MG (1992) Farnesylation of YDJ1p is required for function at elevated growth temperatures in S. cerevisiae. J Biol Chem 267:18890-18895
    • (1992) J Biol Chem , vol.267 , pp. 18890-18895
    • Caplan, A.J.1    Tsai, J.2    Casey, P.J.3    Douglas, M.G.4
  • 12
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaption of chaperone function
    • Cheetham ME, Caplan AJ (1998) Structure, function and evolution of DnaJ: conservation and adaption of chaperone function. Cell Stress Chaperones 3:28-36
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 13
    • 0030930513 scopus 로고    scopus 로고
    • The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae
    • Corsi AK, Schekman R (1997) The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J Cell Biol 137:1483-1493
    • (1997) J Cell Biol , vol.137 , pp. 1483-1493
    • Corsi, A.K.1    Schekman, R.2
  • 14
    • 0036809412 scopus 로고    scopus 로고
    • A specialized mitochondrial molecular chaperone system: A role in formation of Fe/S centers
    • Craig EA, Marszalek J (2002) A specialized mitochondrial molecular chaperone system: a role in formation of Fe/S centers. Cell Mol Life Sci 59:1658-1665
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1658-1665
    • Craig, E.A.1    Marszalek, J.2
  • 15
    • 0038690471 scopus 로고    scopus 로고
    • Ribosome-tethered molecular chaperones: The first line of defense against protein misfolding?
    • Craig EA, Eisenman HC, Hundley HA (2003) Ribosome-tethered molecular chaperones: the first line of defense against protein misfolding? Curr Opin Microbiol 6:157-162
    • (2003) Curr Opin Microbiol , vol.6 , pp. 157-162
    • Craig, E.A.1    Eisenman, H.C.2    Hundley, H.A.3
  • 16
    • 0034671178 scopus 로고    scopus 로고
    • Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli
    • Cupp-Vickery JR, Vickery LE (2000) Crystal structure of Hsc20, a J-type Co-chaperone from Escherichia coli. J Mol Biol 304:835-845
    • (2000) J Mol Biol , vol.304 , pp. 835-845
    • Cupp-Vickery, J.R.1    Vickery, L.E.2
  • 17
    • 7544224771 scopus 로고    scopus 로고
    • Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane
    • D'Silva P, Liu Q, Walter W, Craig EA (2004) Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane. Nat Struct Mol Biol 11:1084-1091
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1084-1091
    • D'Silva, P.1    Liu, Q.2    Walter, W.3    Craig, E.A.4
  • 19
    • 24644486039 scopus 로고    scopus 로고
    • D'Silva P, Schilke B, Walter W, Craig EA (2005) Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane. Proc Natl Acad Sci U S A 102:12419-12424
    • D'Silva P, Schilke B, Walter W, Craig EA (2005) Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane. Proc Natl Acad Sci U S A 102:12419-12424
  • 20
    • 11444271010 scopus 로고    scopus 로고
    • Chaperone-assisted folding of newly synthesized proteins in the cytosol
    • Deuerling E, Bukau B (2004) Chaperone-assisted folding of newly synthesized proteins in the cytosol. Crit Rev Biochem Mol Biol 39:261-277
    • (2004) Crit Rev Biochem Mol Biol , vol.39 , pp. 261-277
    • Deuerling, E.1    Bukau, B.2
  • 22
    • 0042531776 scopus 로고    scopus 로고
    • Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis: Similarities to and differences from its bacterial counterparts
    • Dutkiewicz R, Schilke B, Knieszner H, Walter W, Craig EA, Marszalek J (2003) Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis: similarities to and differences from its bacterial counterparts. J Biol Chem 278:29719-29727
    • (2003) J Biol Chem , vol.278 , pp. 29719-29727
    • Dutkiewicz, R.1    Schilke, B.2    Knieszner, H.3    Walter, W.4    Craig, E.A.5    Marszalek, J.6
  • 23
    • 3142716203 scopus 로고    scopus 로고
    • Sequence specific interactions between mitochondrial Fe/S scaffold protein Isu1 and Hsp70 Ssq1 is essential for their in vivo function
    • Dutkiewicz R, Schilke B, Cheng S, Knieszner H, Craig E, Marszalek J (2004) Sequence specific interactions between mitochondrial Fe/S scaffold protein Isu1 and Hsp70 Ssq1 is essential for their in vivo function. J Biol Chem 279:29167-29174
    • (2004) J Biol Chem , vol.279 , pp. 29167-29174
    • Dutkiewicz, R.1    Schilke, B.2    Cheng, S.3    Knieszner, H.4    Craig, E.5    Marszalek, J.6
  • 24
    • 4344616571 scopus 로고    scopus 로고
    • Mechanism of substrate recognition by Hsp70 chaperones
    • Erbse A, Mayer MP, Bukau B (2004) Mechanism of substrate recognition by Hsp70 chaperones. Biochem Soc Trans 32:617-621
    • (2004) Biochem Soc Trans , vol.32 , pp. 617-621
    • Erbse, A.1    Mayer, M.P.2    Bukau, B.3
  • 25
    • 0742305339 scopus 로고    scopus 로고
    • Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function
    • Fan C, Lee S, Ren H, DM C (2004) Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol Biol Cell 15:761-773
    • (2004) Mol Biol Cell , vol.15 , pp. 761-773
    • Fan, C.1    Lee, S.2    Ren, H.3    DM, C.4
  • 26
    • 1242269219 scopus 로고    scopus 로고
    • Mechanisms for regulation of Hsp70 function by Hsp40
    • Fan CY, Lee S, Cyr DM (2003) Mechanisms for regulation of Hsp70 function by Hsp40. Cell Stress Chaperones 8:309-316
    • (2003) Cell Stress Chaperones , vol.8 , pp. 309-316
    • Fan, C.Y.1    Lee, S.2    Cyr, D.M.3
  • 27
    • 12844277294 scopus 로고    scopus 로고
    • The type I Hsp40 zinc finger-like region is required for Hsp70 to capture non-native polypeptides from Ydj1
    • Fan CY, Ren HY, Lee P, Caplan AJ, Cyr DM (2005) The type I Hsp40 zinc finger-like region is required for Hsp70 to capture non-native polypeptides from Ydj1. J Biol Chem 280:695-702
    • (2005) J Biol Chem , vol.280 , pp. 695-702
    • Fan, C.Y.1    Ren, H.Y.2    Lee, P.3    Caplan, A.J.4    Cyr, D.M.5
  • 28
    • 0026690820 scopus 로고
    • Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation
    • Feldheim D, Rothblatt J, Schekman R (1992) Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation. Mol Cell Biol 12:3288-3296
    • (1992) Mol Cell Biol , vol.12 , pp. 3288-3296
    • Feldheim, D.1    Rothblatt, J.2    Schekman, R.3
  • 29
    • 10344227184 scopus 로고    scopus 로고
    • Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating
    • Fotin A, Cheng Y, Grigorieff N, Walz T, Harrison SC, Kirchhausen T (2004a) Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating. Nature 432:649-653
    • (2004) Nature , vol.432 , pp. 649-653
    • Fotin, A.1    Cheng, Y.2    Grigorieff, N.3    Walz, T.4    Harrison, S.C.5    Kirchhausen, T.6
  • 33
    • 0030044799 scopus 로고    scopus 로고
    • A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma 32
    • Gamer J, Multhaup G, Tomoyasu T, McCarty JS, Rudiger S, Schonfeld HJ, Schirra C, Bujard H, Bukau B (1996) A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma 32. EMBO J 15:607-617
    • (1996) EMBO J , vol.15 , pp. 607-617
    • Gamer, J.1    Multhaup, G.2    Tomoyasu, T.3    McCarty, J.S.4    Rudiger, S.5    Schonfeld, H.J.6    Schirra, C.7    Bujard, H.8    Bukau, B.9
  • 35
    • 0036859957 scopus 로고    scopus 로고
    • Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain
    • Genevaux P, Schwager F, Georgopoulos C, Kelley WL (2002) Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain. Genetics 162:1045-1053
    • (2002) Genetics , vol.162 , pp. 1045-1053
    • Genevaux, P.1    Schwager, F.2    Georgopoulos, C.3    Kelley, W.L.4
  • 36
    • 0032568541 scopus 로고    scopus 로고
    • Role of the J-domain in the cooperation of Hsp40 with Hsp70
    • Greene M, Maskos K, Landry S (1998) Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proc Natl Acad Sci U S A 95:6108-6113
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6108-6113
    • Greene, M.1    Maskos, K.2    Landry, S.3
  • 37
    • 1542638696 scopus 로고    scopus 로고
    • Structure of the functional fragment of auxilin required for catalytic uncoating of clathrin-coated vesicles
    • Gruschus JM, Han CJ, Greener T, Ferretti JA, Greene LE, Eisenberg E (2004) Structure of the functional fragment of auxilin required for catalytic uncoating of clathrin-coated vesicles. Biochemistry 43:3111-3119
    • (2004) Biochemistry , vol.43 , pp. 3111-3119
    • Gruschus, J.M.1    Han, C.J.2    Greener, T.3    Ferretti, J.A.4    Greene, L.E.5    Eisenberg, E.6
  • 38
    • 0037928428 scopus 로고    scopus 로고
    • Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system
    • Han W, Christen P (2003) Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system. J Biol Chem 278:19038-19043
    • (2003) J Biol Chem , vol.278 , pp. 19038-19043
    • Han, W.1    Christen, P.2
  • 39
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276:431-435
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.4    Kuriyan, J.5
  • 40
    • 0028073776 scopus 로고
    • Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA
    • Hermann J, Stuart R, Craig E, Neupert W (1994) Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA. J Cell Biol 127:893-902
    • (1994) J Cell Biol , vol.127 , pp. 893-902
    • Hermann, J.1    Stuart, R.2    Craig, E.3    Neupert, W.4
  • 41
    • 8744269767 scopus 로고    scopus 로고
    • Tail-anchored protein biosynthesis at the endoplasmic reticulum: The same but different
    • High S, Abell BM (2004) Tail-anchored protein biosynthesis at the endoplasmic reticulum: the same but different. Biochem Soc Trans 32:659-662
    • (2004) Biochem Soc Trans , vol.32 , pp. 659-662
    • High, S.1    Abell, B.M.2
  • 42
    • 0034608935 scopus 로고    scopus 로고
    • Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli
    • Hoff KG, Silberg JJ, Vickery LE (2000) Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli. Proc Natl Acad Sci U S A 97:7790-7795
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 7790-7795
    • Hoff, K.G.1    Silberg, J.J.2    Vickery, L.E.3
  • 43
    • 0037178878 scopus 로고    scopus 로고
    • Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU
    • Hoff KG, Ta DT, Tapley TL, Silberg JJ, Vickery LE (2002) Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU. J Biol Chem 277:27353-27359
    • (2002) J Biol Chem , vol.277 , pp. 27353-27359
    • Hoff, K.G.1    Ta, D.T.2    Tapley, T.L.3    Silberg, J.J.4    Vickery, L.E.5
  • 44
    • 0029846829 scopus 로고    scopus 로고
    • Mechanism of clathrin basket dissociation: Separate functions of protein domains of the DnaJ homologue auxilin
    • Holstein SE, Ungewickell H, Ungewickell E (1996) Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin. J Cell Biol 135:925-937
    • (1996) J Cell Biol , vol.135 , pp. 925-937
    • Holstein, S.E.1    Ungewickell, H.2    Ungewickell, E.3
  • 45
    • 0032947385 scopus 로고    scopus 로고
    • The influence of C-terminal extension on the structure of the "J-domain" in E. coli DnaJ
    • Huang K, Flanagan JM, Prestegard JH (1999) The influence of C-terminal extension on the structure of the "J-domain" in E. coli DnaJ. Prot Sci 8:203-214
    • (1999) Prot Sci , vol.8 , pp. 203-214
    • Huang, K.1    Flanagan, J.M.2    Prestegard, J.H.3
  • 46
    • 22444439361 scopus 로고    scopus 로고
    • The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1
    • Huang P, Gautschi M, Walter W, Rospert S, Craig EA (2005) The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat Struct Mol Biol 12:497-504
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 497-504
    • Huang, P.1    Gautschi, M.2    Walter, W.3    Rospert, S.4    Craig, E.A.5
  • 48
    • 18644382616 scopus 로고    scopus 로고
    • Hundley HA, Walter W, Bairstow S, Craig EA (2005) Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous. Science 308:1032-1034
    • Hundley HA, Walter W, Bairstow S, Craig EA (2005) Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous. Science 308:1032-1034
  • 49
    • 4444355303 scopus 로고    scopus 로고
    • Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein
    • Huyer G, Piluek WF, Fansler Z, Kreft SG, Hochstrasser M, Brodsky JL, Michaelis S (2004) Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J Biol Chem 279:38369-38378
    • (2004) J Biol Chem , vol.279 , pp. 38369-38378
    • Huyer, G.1    Piluek, W.F.2    Fansler, Z.3    Kreft, S.G.4    Hochstrasser, M.5    Brodsky, J.L.6    Michaelis, S.7
  • 51
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson DC, Dean DR, Smith AD, Johnson MK (2005) Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem 74:247-281
    • (2005) Annu Rev Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 52
    • 0035911158 scopus 로고    scopus 로고
    • An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae
    • Johnson JL, Craig EA (2001) An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae. J Cell Biol 52:851-856
    • (2001) J Cell Biol , vol.52 , pp. 851-856
    • Johnson, J.L.1    Craig, E.A.2
  • 53
    • 0032573163 scopus 로고    scopus 로고
    • Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
    • Kim S, Schilke B, Craig E, Horwich A (1998) Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci U S A 95:12860-12865
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12860-12865
    • Kim, S.1    Schilke, B.2    Craig, E.3    Horwich, A.4
  • 56
    • 0035951385 scopus 로고    scopus 로고
    • Mitochondrial Hsp78, a member of the C1p/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding
    • Krzewska J, Langer T, Liberek K (2001) Mitochondrial Hsp78, a member of the C1p/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding. FEBS Lett 489:92-96
    • (2001) FEBS Lett , vol.489 , pp. 92-96
    • Krzewska, J.1    Langer, T.2    Liberek, K.3
  • 57
    • 18844374988 scopus 로고    scopus 로고
    • Swivels and stators in the Hsp40-Hsp70 chaperone machine
    • Landry S (2003) Swivels and stators in the Hsp40-Hsp70 chaperone machine. Structure 8:799-807
    • (2003) Structure , vol.8 , pp. 799-807
    • Landry, S.1
  • 58
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ, and GroEL along the pathway of chaperone-mediated protein folding
    • Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU (1992) Successive action of DnaK, DnaJ, and GroEL along the pathway of chaperone-mediated protein folding. Nature 356:683-089
    • (1992) Nature , vol.356 , pp. 683-089
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 59
    • 0345299781 scopus 로고    scopus 로고
    • The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate
    • Li J, Qian X, Sha B (2003) The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure 11:1475-1483
    • (2003) Structure , vol.11 , pp. 1475-1483
    • Li, J.1    Qian, X.2    Sha, B.3
  • 60
    • 4444315535 scopus 로고    scopus 로고
    • The presequence translocase-associated protein import motor of mitochondria. Pam16 functions in an antagonistic manner to Pam18
    • Li Y, Dudek J, Guiard B, Pfanner N, Rehling P, Voos W (2004) The presequence translocase-associated protein import motor of mitochondria. Pam16 functions in an antagonistic manner to Pam18. J Biol Chem 279:38047-38054
    • (2004) J Biol Chem , vol.279 , pp. 38047-38054
    • Li, Y.1    Dudek, J.2    Guiard, B.3    Pfanner, N.4    Rehling, P.5    Voos, W.6
  • 61
    • 0029052538 scopus 로고
    • The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator
    • Liberek K, Wall D, Georgopoulos C (1995) The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator. Proc Natl Acad Sci U S A 92:6224-6228
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 6224-6228
    • Liberek, K.1    Wall, D.2    Georgopoulos, C.3
  • 62
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • Lill R, Muhlenhoff U (2005) Iron-sulfur-protein biogenesis in eukaryotes. Trends Biochem Sci 30:133-141
    • (2005) Trends Biochem Sci , vol.30 , pp. 133-141
    • Lill, R.1    Muhlenhoff, U.2
  • 63
  • 64
    • 0035794158 scopus 로고    scopus 로고
    • Mitochondrial Hsp70 Ssc1: Role in protein folding
    • Liu Q, Krzewska J, Liberek K, Craig EA (2001) Mitochondrial Hsp70 Ssc1: role in protein folding. J Biol Chem 276:6112-6118
    • (2001) J Biol Chem , vol.276 , pp. 6112-6118
    • Liu, Q.1    Krzewska, J.2    Liberek, K.3    Craig, E.A.4
  • 65
    • 0037345064 scopus 로고    scopus 로고
    • Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ(+)]
    • Lopez N, Aron R, Craig EA (2003) Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ(+)]. Mol Biol Cell 14:1172-1181
    • (2003) Mol Biol Cell , vol.14 , pp. 1172-1181
    • Lopez, N.1    Aron, R.2    Craig, E.A.3
  • 66
    • 0032489556 scopus 로고    scopus 로고
    • The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding
    • Lu Z, Cyr DM (1998a) The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding. J Biol Chem 273:5970-5978
    • (1998) J Biol Chem , vol.273 , pp. 5970-5978
    • Lu, Z.1    Cyr, D.M.2
  • 67
    • 0032561360 scopus 로고    scopus 로고
    • Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1
    • Lu Z, Cyr DM (1998b) Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1. J Biol Chem 273:27824-27830
    • (1998) J Biol Chem , vol.273 , pp. 27824-27830
    • Lu, Z.1    Cyr, D.M.2
  • 68
    • 0030970268 scopus 로고    scopus 로고
    • Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP
    • Lyman SK, Schekman R (1997) Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88:85-96
    • (1997) Cell , vol.88 , pp. 85-96
    • Lyman, S.K.1    Schekman, R.2
  • 69
    • 0034698002 scopus 로고    scopus 로고
    • Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ
    • Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ (2000) Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. J Mol Biol 300:805-818
    • (2000) J Mol Biol , vol.300 , pp. 805-818
    • Martinez-Yamout, M.1    Legge, G.B.2    Zhang, O.3    Wright, P.E.4    Dyson, H.J.5
  • 70
  • 71
    • 0033785942 scopus 로고    scopus 로고
    • Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum
    • McClellan AJ, Brodsky JL (2000) Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum. Genetics 156:501-512
    • (2000) Genetics , vol.156 , pp. 501-512
    • McClellan, A.J.1    Brodsky, J.L.2
  • 72
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham GC, Lu Z, King S, Sorscher E, Tousson A, Cyr DM (1999) The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J 18:1492-1505
    • (1999) EMBO J , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 74
    • 0033575256 scopus 로고    scopus 로고
    • Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex
    • Misselwitz B, Staeck O, Matlack KE, Rapoport TA (1999) Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex. J Biol Chem 274:20110-20115
    • (1999) J Biol Chem , vol.274 , pp. 20110-20115
    • Misselwitz, B.1    Staeck, O.2    Matlack, K.E.3    Rapoport, T.A.4
  • 75
    • 0141865519 scopus 로고    scopus 로고
    • Tim14, a novel key component of the import motor of the Tim23 protein translocase of mitochondria
    • Mokranjac D, Sichting M, Neupert W, Hell K (2003) Tim14, a novel key component of the import motor of the Tim23 protein translocase of mitochondria. EMBO J 22:4945-4956
    • (2003) EMBO J , vol.22 , pp. 4945-4956
    • Mokranjac, D.1    Sichting, M.2    Neupert, W.3    Hell, K.4
  • 76
    • 0030581175 scopus 로고    scopus 로고
    • NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone
    • Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wuthrich K (1996) NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J Mol Biol 260:236-250
    • (1996) J Mol Biol , vol.260 , pp. 236-250
    • Pellecchia, M.1    Szyperski, T.2    Wall, D.3    Georgopoulos, C.4    Wuthrich, K.5
  • 77
    • 0033671314 scopus 로고    scopus 로고
    • Pishvaee B, Costaguta G, Yeung BG, Ryazantsev S, Greener T, Greene LE, Eisenberg E, McCaffery JM, Payne GS (2000) A yeast DNA J protein required for uncoating of clathrin-coated vesicles in vivo. Nat Cell Biol 2:958-963
    • Pishvaee B, Costaguta G, Yeung BG, Ryazantsev S, Greener T, Greene LE, Eisenberg E, McCaffery JM, Payne GS (2000) A yeast DNA J protein required for uncoating of clathrin-coated vesicles in vivo. Nat Cell Biol 2:958-963
  • 78
    • 0035007292 scopus 로고    scopus 로고
    • Cloning, expression, purification and preliminary X-ray crystallographic studies of yeast Hsp40 Sis1 complexed with Hsp70 Ssa1 C-terminal lid domain
    • Qian X, Li Z, Sha B (2001) Cloning, expression, purification and preliminary X-ray crystallographic studies of yeast Hsp40 Sis1 complexed with Hsp70 Ssa1 C-terminal lid domain. Acta Crystallogr D Biol Crystallogr 57:748-750
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 748-750
    • Qian, X.1    Li, Z.2    Sha, B.3
  • 79
    • 0036177548 scopus 로고    scopus 로고
    • Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: Yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1
    • Qian X, Hou W, Zhengang L, Sha B (2002) Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1. Biochem J 361:27-34
    • (2002) Biochem J , vol.361 , pp. 27-34
    • Qian, X.1    Hou, W.2    Zhengang, L.3    Sha, B.4
  • 80
    • 0030581148 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain
    • Qian YQ, Patel D, Hartl FU, McColl DJ (1996) Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J Mol Biol 260:224-235
    • (1996) J Mol Biol , vol.260 , pp. 224-235
    • Qian, Y.Q.1    Patel, D.2    Hartl, F.U.3    McColl, D.J.4
  • 82
    • 0028284879 scopus 로고
    • Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
    • Rowley N, Prip-Buus C, Westermann B, Brown C, Schwarz E, Barrell B, Neupert W (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77:249-259
    • (1994) Cell , vol.77 , pp. 249-259
    • Rowley, N.1    Prip-Buus, C.2    Westermann, B.3    Brown, C.4    Schwarz, E.5    Barrell, B.6    Neupert, W.7
  • 83
    • 0035283043 scopus 로고    scopus 로고
    • Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
    • Rudiger S, Schneider-Mergener J, Bukau B (2001) Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J 20:1042-1050
    • (2001) EMBO J , vol.20 , pp. 1042-1050
    • Rudiger, S.1    Schneider-Mergener, J.2    Bukau, B.3
  • 84
    • 0029021905 scopus 로고
    • A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s
    • Schlenstedt G, Harris S, Risse B, Lill R, Silver PA (1995) A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J Cell Biol 129:979-988
    • (1995) J Cell Biol , vol.129 , pp. 979-988
    • Schlenstedt, G.1    Harris, S.2    Risse, B.3    Lill, R.4    Silver, P.A.5
  • 85
    • 0034662746 scopus 로고    scopus 로고
    • The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1
    • Sha B, Lee S, Cyr DM (2000) The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. Structure Fold Des 8:799-807
    • (2000) Structure Fold Des , vol.8 , pp. 799-807
    • Sha, B.1    Lee, S.2    Cyr, D.M.3
  • 86
    • 0032539016 scopus 로고    scopus 로고
    • A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum
    • Silberstein S, Schlenstedt G, Silver PA, Gilmore R (1998) A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum. J Cell Biol 143:921-933
    • (1998) J Cell Biol , vol.143 , pp. 921-933
    • Silberstein, S.1    Schlenstedt, G.2    Silver, P.A.3    Gilmore, R.4
  • 87
    • 0036049850 scopus 로고    scopus 로고
    • The unfolding story of the Escherichia coli Hsp70 DnaK: Is DnaK a holdase or an unfoldase?
    • Slepenkov SV, Witt SN (2002) The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase? Mol Microbiol 45:1197-1206
    • (2002) Mol Microbiol , vol.45 , pp. 1197-1206
    • Slepenkov, S.V.1    Witt, S.N.2
  • 90
    • 0041734594 scopus 로고    scopus 로고
    • Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ
    • Suh WC, Lu CZ, Gross CA (1999) Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ. J Biol Chem 274:30534-30539
    • (1999) J Biol Chem , vol.274 , pp. 30534-30539
    • Suh, W.C.1    Lu, C.Z.2    Gross, C.A.3
  • 92
    • 0029871766 scopus 로고    scopus 로고
    • A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding
    • Tsai J, Douglas MG (1996) A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. J Biol Chem 271:9347-9354
    • (1996) J Biol Chem , vol.271 , pp. 9347-9354
    • Tsai, J.1    Douglas, M.G.2
  • 95
    • 0027946910 scopus 로고
    • Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded protein in mitochondria
    • Wagner I, Arlt H, van Dyck L, Langer T, Neupert T (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded protein in mitochondria. EMBO J 13:5135-5145
    • (1994) EMBO J , vol.13 , pp. 5135-5145
    • Wagner, I.1    Arlt, H.2    van Dyck, L.3    Langer, T.4    Neupert, T.5
  • 96
    • 0028170215 scopus 로고
    • The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication
    • Wall D, Zylicz M, Georgopoulos C (1994) The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication. J Biol Chem 269:5446-5451
    • (1994) J Biol Chem , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 97
    • 0028930540 scopus 로고
    • The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone
    • Wall D, Zylicz M, Georgopoulos C (1995) The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone. J Biol Chem 270:2139-2144
    • (1995) J Biol Chem , vol.270 , pp. 2139-2144
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 98
    • 4344590764 scopus 로고    scopus 로고
    • The J-protein family: Modulating protein assembly, disassembly and translocation
    • Walsh P, Bursac D, Law YC, Cyr D, Lithgow T (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5:567-571
    • (2004) EMBO Rep , vol.5 , pp. 567-571
    • Walsh, P.1    Bursac, D.2    Law, Y.C.3    Cyr, D.4    Lithgow, T.5
  • 99
    • 0031551576 scopus 로고    scopus 로고
    • Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast
    • Westermann B, Neupert W (1997) Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast. J Mol Biol 272:477-483
    • (1997) J Mol Biol , vol.272 , pp. 477-483
    • Westermann, B.1    Neupert, W.2
  • 100
    • 0038523841 scopus 로고    scopus 로고
    • The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70
    • Wittung-Stafshede P, Guidry J, Horne BE, Landry SJ (2003) The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70. Biochemistry 42:4937-4944
    • (2003) Biochemistry , vol.42 , pp. 4937-4944
    • Wittung-Stafshede, P.1    Guidry, J.2    Horne, B.E.3    Landry, S.J.4
  • 101
    • 13444274413 scopus 로고    scopus 로고
    • The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40
    • Wu Y, Li J, Jin Z, Fu Z, Sha B (2005) The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40. J Mol Biol 346:1005-1011
    • (2005) J Mol Biol , vol.346 , pp. 1005-1011
    • Wu, Y.1    Li, J.2    Jin, Z.3    Fu, Z.4    Sha, B.5
  • 102
    • 0032694248 scopus 로고    scopus 로고
    • The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1
    • Yan W, Craig EA (1999) The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1. Mol Cell Biol 19:7751-7758
    • (1999) Mol Cell Biol , vol.19 , pp. 7751-7758
    • Yan, W.1    Craig, E.A.2
  • 104
    • 6344275303 scopus 로고    scopus 로고
    • Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
    • Youker RT, Walsh P, Beilharz T, Lithgow T, Brodsky JL (2004) Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol Biol Cell 15:4787-4797
    • (2004) Mol Biol Cell , vol.15 , pp. 4787-4797
    • Youker, R.T.1    Walsh, P.2    Beilharz, T.3    Lithgow, T.4    Brodsky, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.