메뉴 건너뛰기




Volumn 169, Issue 4, 2005, Pages 1873-1882

In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; PROTEIN SIS1; UNCLASSIFIED DRUG;

EID: 18844400606     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: 10.1534/genetics.104.037242     Document Type: Article
Times cited : (45)

References (33)
  • 1
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • BUKAU, B., and A. L. HORWICH, 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
  • 2
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: Conservation and adaption of chaperone function
    • CHEETHAM, M. E., and A. J. CAPLAN, 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
  • 3
    • 2642689664 scopus 로고    scopus 로고
    • The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors
    • DEMAND, J., J. LUDERS and J. HOHFELD, 1998 The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Mol. Cell. Biol. 18: 2023-2028.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2023-2028
    • Demand, J.1    Luders, J.2    Hohfeld, J.3
  • 4
    • 0742305339 scopus 로고    scopus 로고
    • Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function
    • FAN, C., S. LEE, H. REN and D. M. CYR, 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    Cyr, D.M.4
  • 6
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/ SS-DNA/PEG procedure
    • GIETZ, R. D., R. H. SCHIESTL, A. R. WILLEMS and R. A. WOODS, 1995 Studies on the transformation of intact yeast cells by the LiAc/ SS-DNA/PEG procedure. Yeast 11: 355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 7
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • GUAN, K. L., and J. E. DIXON, 1991 Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192: 262-267.
    • (1991) Anal. Biochem. , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 8
    • 0032947385 scopus 로고    scopus 로고
    • The influence of C-terminal extension on the structure of the "J-domain" in E. coli DnaJ
    • HUANG, K., J. M. FLANAGAN and J. H. PRESTEGARD, 1999 The influence of C-terminal extension on the structure of the "J-domain" in E. coli DnaJ. Protein Sci. 8: 203-214.
    • (1999) Protein Sci. , vol.8 , pp. 203-214
    • Huang, K.1    Flanagan, J.M.2    Prestegard, J.H.3
  • 9
    • 0035911158 scopus 로고    scopus 로고
    • An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae
    • JOHNSON, J. L., and E. A. CRAIG, 2001 An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae. J. Cell Biol. 152: 851-856.
    • (2001) J. Cell Biol. , vol.152 , pp. 851-856
    • Johnson, J.L.1    Craig, E.A.2
  • 10
    • 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
  • 12
    • 0037077211 scopus 로고    scopus 로고
    • Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding
    • LEE, S., C. FAN, J. YOUNGER, H. REN and D. CYR, 2002 Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding. J. Biol. Chem. 277: 21675-21682.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21675-21682
    • Lee, S.1    Fan, C.2    Younger, J.3    Ren, H.4    Cyr, D.5
  • 13
    • 0345299781 scopus 로고    scopus 로고
    • The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate
    • Li, J., X. QIAN and B. SHA, 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
  • 14
  • 15
    • 0035794158 scopus 로고    scopus 로고
    • Mitochondrial Hsp70 Ssc1: Role in protein folding
    • LIU, Q., J. KRZEWSKA, K. LIBEREK and E. A. CRAIG, 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
  • 16
    • 0037345064 scopus 로고    scopus 로고
    • Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ(+)]
    • LOPEZ, N., R. ARON and E. A. CRAIG, 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
  • 17
    • 0032561360 scopus 로고    scopus 로고
    • Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1
    • Lu, Z., and D. M. CYR, 1998 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
  • 18
    • 0025824364 scopus 로고
    • Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins
    • LUKE, M., A. SUTTIN and K. ARNDT, 1991 Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins. J. Cell Biol. 114: 623-638.
    • (1991) J. Cell Biol. , vol.114 , pp. 623-638
    • Luke, M.1    Suttin, A.2    Arndt, K.3
  • 19
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • MUMBERG, D., R. MULLER and M. FUNK, 1995 Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156: 119-122.
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 20
    • 0035658334 scopus 로고    scopus 로고
    • Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared to other Hsp70s
    • PFUND, C., P. HUANG, N. LOPEZ-HOYO and E. CRAIG, 2001 Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared to other Hsp70s. Mol. Biol. Cell 12: 3773-3782.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3773-3782
    • Pfund, C.1    Huang, P.2    Lopez-Hoyo, N.3    Craig, E.4
  • 21
    • 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., W. Hou, L. ZHENGANG and B. SHA, 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
  • 22
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • SERIO, T. R., A. G. CASHIKAR, A. S. KOWAL, G. J. SAWICKI, J. J. MOSLEHI et al., 2000 Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289: 1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5
  • 23
    • 0034662746 scopus 로고    scopus 로고
    • The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1
    • SHA, B., S. LEE and D. M. CYR, 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
  • 24
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • SIKORSKI, R. S., and P. HIETER, 1989 A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 25
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: An epigenetic modifier of protein function in yeast
    • SONDHEIMER, N., and S. LINDQUIST, 2000 Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell 5: 163-172.
    • (2000) Mol. Cell , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 26
    • 0035873740 scopus 로고    scopus 로고
    • The role of Sis1 in the maintenance of the [RNQ+] prion
    • SONDHEIMER, N., N. LOPEZ, E. A. CRAIG and S. LINDQUIST, 2001 The role of Sis1 in the maintenance of the [RNQ+] prion. EMBO J. 20: 2435-2442.
    • (2001) EMBO J. , vol.20 , pp. 2435-2442
    • Sondheimer, N.1    Lopez, N.2    Craig, E.A.3    Lindquist, S.4
  • 27
    • 0032417526 scopus 로고    scopus 로고
    • Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ
    • SUH, W.-C., W. BURKHOLDER, C. Z. LU, X. ZHAO, M. GOTTESMAN et al., 1998 Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ. Proc. Natl. Acad. Sci. USA 95: 15223-15228.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15223-15228
    • Suh, W.-C.1    Burkholder, W.2    Lu, C.Z.3    Zhao, X.4    Gottesman, M.5
  • 28
    • 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., M. ZYLICZ and C. GEORGOPOULOS, 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
  • 29
    • 0029094250 scopus 로고
    • Divergent effects of ATP on the binding of the DnaK and DnaJ chape rones to each other, or to their various native and denatured protein substrates
    • WAWRZYNOW, A., and M. ZYLICZ, 1995 Divergent effects of ATP on the binding of the DnaK and DnaJ chape rones to each other, or to their various native and denatured protein substrates. J. Biol. Chem. 270: 19300-19306.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19300-19306
    • Wawrzynow, A.1    Zylicz, M.2
  • 31
    • 0032694248 scopus 로고    scopus 로고
    • The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1
    • YAN, W., and E. A. CRAIG, 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
  • 32
    • 5044239107 scopus 로고    scopus 로고
    • Pathways of chaperone-mediated protein folding in the cytosol
    • YOUNG, J., V. AGASHE, K. SIEGERS and F. HARTL, 2004 Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev. Mol. Cell Biol. 5: 781-791.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 781-791
    • Young, J.1    Agashe, V.2    Siegers, K.3    Hartl, F.4
  • 33
    • 0027256768 scopus 로고
    • The yeast SIS1 protein, a DnaJ homolog, is required for initiation of translation
    • ZHONG, T., and K. T. ARNDT, 1993 The yeast SIS1 protein, a DnaJ homolog, is required for initiation of translation. Cell 73: 1175-1186.
    • (1993) Cell , vol.73 , pp. 1175-1186
    • Zhong, T.1    Arndt, K.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.