메뉴 건너뛰기




Volumn 6, Issue 1, 2004, Pages 204-208

Peptide substrate identification for yeast Hsp40 Ydj1 by screening the phage display library

Author keywords

Heat shock proteins 70; Molecular chaperones; Peptide library; Protein folding

Indexed keywords

CHAPERONE; FUNGAL PROTEIN; HEAT SHOCK PROTEIN 40;

EID: 25444495617     PISSN: 14809222     EISSN: None     Source Type: Journal    
DOI: 10.1251/bpo90     Document Type: Article
Times cited : (9)

References (23)
  • 1
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell 1998; 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 2
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU. Molecular chaperones in cellular protein folding. Nature 1996; 381:571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 3
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002; 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 4
    • 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. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 1992; 356:683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 7
    • 0032214832 scopus 로고    scopus 로고
    • J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
    • Misselwitz S, Staeck O, Rapoport TA. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol Cell 1998; 2:593-603.
    • (1998) Mol. Cell. , vol.2 , pp. 593-603
    • Misselwitz, S.1    Staeck, O.2    Rapoport, T.A.3
  • 8
    • 0036177548 scopus 로고    scopus 로고
    • Direct interactions between molecular chaperones Hsp70 and Hsp40: Yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1
    • Qian X, Hou W, Li Z, Sha BD. Direct interactions between molecular chaperones Hsp70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1. Biochem J 2002; 361:27-34.
    • (2002) Biochem. J. , vol.361 , pp. 27-34
    • Qian, X.1    Hou, W.2    Li, Z.3    Sha, B.D.4
  • 9
    • 0028170215 scopus 로고
    • The N-terminal 108 amino acids of the E. coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lamda replication
    • Wall D, Zylicz M, Georgopoulos C. The N-terminal 108 amino acids of the E. coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lamda replication. J Biol Chem 1994; 269:5446-5451.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 10
    • 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. The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding. J Biol Chem 1998; 273:5970-5978.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5970-5978
    • Lu, Z.1    Cyr, D.M.2
  • 11
    • 0025745326 scopus 로고
    • Characterization of Ydj1: A yeast homologue of the bacteria dnaJ protein
    • Caplan AJ, Douglas MG. Characterization of Ydj1: a yeast homologue of the bacteria dnaJ protein. J Cell Biol 1991; 114:609-621.
    • (1991) J. Cell Biol. , vol.114 , pp. 609-621
    • Caplan, A.J.1    Douglas, M.G.2
  • 12
    • 0032561360 scopus 로고    scopus 로고
    • Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperone Sis1 and Ydj1
    • Lu Z, Cyr DM. Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperone Sis1 and Ydj1. J Biol Chem 1998; 273:27824-27830.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27824-27830
    • Lu, Z.1    Cyr, D.M.2
  • 13
    • 0030030946 scopus 로고    scopus 로고
    • A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates
    • Szabo A, Korszun R, Hartl FU, Flanagan J. A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J 1996; 15:408-417.
    • (1996) EMBO J. , vol.15 , pp. 408-417
    • Szabo, A.1    Korszun, R.2    Hartl, F.U.3    Flanagan, J.4
  • 14
    • 0035911158 scopus 로고    scopus 로고
    • An essential role for the substratebinding region of Hsp40s in Saccharomyces cerevisiae
    • Johnson JL, Craig EA. An essential role for the substratebinding region of Hsp40s in Saccharomyces cerevisiae. J Cell Biol 2001; 152:851-856.
    • (2001) J. Cell Biol. , vol.152 , pp. 851-856
    • Johnson, J.L.1    Craig, E.A.2
  • 15
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone Bip
    • Flynn GC, Pohl J, Flocco MT, Rothman JE. Peptide-binding specificity of the molecular chaperone Bip. Nature 1991; 353:726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 17
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide comlex: Plasticity as a basis for substrate diversity
    • Chen L, Sigler PB. The crystal structure of a GroEL/peptide comlex: plasticity as a basis for substrate diversity. Cell 1999; 99:757-768.
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 18
    • 0034662746 scopus 로고    scopus 로고
    • The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1
    • Sha BD, Lee S, Cyr DM. The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. Structure 2000; 8:799-807.
    • (2000) Structure , vol.8 , pp. 799-807
    • Sha, B.D.1    Lee, S.2    Cyr, D.M.3
  • 19
    • 0345299781 scopus 로고    scopus 로고
    • The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate
    • Li J, Qian X, Sha B. The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure 2003; 11:1475-1483.
    • (2003) Structure , vol.11 , pp. 1475-1483
    • Li, J.1    Qian, X.2    Sha, B.3
  • 20
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott JK, Smith GP. Searching for peptide ligands with an epitope library. Science 1990; 249:386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 21
    • 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. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J 2001; 20:1042-1050.
    • (2001) EMBO J. , vol.20 , pp. 1042-1050
    • Rudiger, S.1    Schneider-Mergener, J.2    Bukau, B.3
  • 22
    • 0032524646 scopus 로고    scopus 로고
    • D-peptide ligands for the co-chaperone DnaJ
    • Feifel B, Schonfeld HJ, Christen P. D-peptide ligands for the co-chaperone DnaJ. J Biol Chem 1998; 273:11999-12002.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11999-12002
    • Feifel, B.1    Schonfeld, H.J.2    Christen, P.3
  • 23
    • 0141613640 scopus 로고    scopus 로고
    • TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes
    • Siegers K, Bolter B, Schwarz JP, Bottcher UM, Guha S, Hartl FU. TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 2003; 22: 5230-5240.
    • (2003) EMBO J. , vol.22 , pp. 5230-5240
    • Siegers, K.1    Bolter, B.2    Schwarz, J.P.3    Bottcher, U.M.4    Guha, S.5    Hartl, F.U.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.