Molecular chaperones: How J domains turn on Hsp70s

Current Biology

Volumn 9, Issue 8, 1999, Pages

  Kelley, William L ^a  

^a UNIVERSITY OF GENEVA   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0033594405     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80185-7     Document Type: Note

References (16)

1. 1. Bukau B, Norwich AL: The Hsp70 and Hsp60 chaperone machines. Cell 1998, 92:351-366.
2. 2. Rüdiger S, Buchberger A, Bukau B: Interaction of Hsp70 chaperones with substrates. Nat Struct Biol 1997, 4:342-349.
3. 3. Mayer MP, Bukau B: Hsp70 chaperone systems: diversity of cellular functions and mechanism of action. Biol Chem 1998, 379:261-268.
4. 4. Takayama S, Xie Z, Reed JC: An evolutionary conserved family of Hsp70/Hsc70 molecular chaperone regulators. J Biol Chem 1999, 274:781-786.
5. 5. Kelley WL: The J-domain family and the recruitment of chaperone power. Trends Biochem Sci 1998, 23:222-227.
6. 6. Schlendstedt G, Harris S, Risse B, Lill R, Silver PA: A yeast DnaJ homolog, scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J Cell Biol 1995, 129:979-988.
7. 7. McClellan AJ, Endres JB, Vogel JP, Palazzi D, Rose MD, Brodsky JL: Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER. Mol Biol Cell 1998, 9:3533-3545.
8. 8. Brodsky JL, Bäurele M, Horst M, McClellan AJ: Mitochondrial Hsp70 cannot replace BiP in driving protein translocation into the yeast endoplasmic reticulum. FEBS Lett 1998, 435:183-186.
9. 9. Lu Z, Cyr, DM: Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1. J Biol Chem 1998, 273:27824-27830.
10. 10. Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wüthrich K: NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J Mol Biol 1996, 260:236-250.
11. 11. Greene MK, Maskos K, Landry SJ: Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proc Natl Acad Sci USA 1998, 95:6108-6113.
12. 12. Karzai AW, McMacken R: A bipartite signalling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J Biol Chem 1996, 271:1 1236-11246.
13. 13. Demand J, Lüders J, Höhfeld J: The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors. Mol Cell Biol 1998, 18:2023-2028.
14. 14. Gässler CS, Buchberger A, Laufen T, Mayer MP, Schröder H, Valencia A, Bukau B: Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone. Proc Natl Acad Sci USA 1998, 95:15229-15234.
15. 15. Suh W-C, Burkholder WF, Lu CZ, Gottesman ME, Gross CA: Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ. Proc Natl Acad Sci USA 1998, 95:15223-15228.
16. 16. Misselwitz B, Staeck O, Rapoport TA: J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol Cell 1998, 2:593-603.