The J-Domain of Hsp40 Couples ATP Hydrolysis to Substrate Capture in Hsp70

The Escherichia coli Hsp40 DnaJ uses its J-domain to target substrate polypeptides for binding to the Hsp70 DnaK, but the mechanism of J-domain function has been obscured by a substrate-like interaction between DnaJ and DnaK. ATP hydrolysis in DnaK is associated with a conformational change that cap...

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Veröffentlicht in:	Biochemistry (Easton) 2003-05, Vol.42 (17), p.4937-4944
Hauptverfasser:	Wittung-Stafshede, Pernilla, Guidry, Jesse, Horne, B. Erin, Landry, Samuel J
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Amino Acid Substitution Binding Sites Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Heat-Shock Proteins - metabolism HSP40 Heat-Shock Proteins HSP70 Heat-Shock Proteins - chemistry HSP70 Heat-Shock Proteins - metabolism Kinetics Models, Molecular Mutagenesis, Site-Directed Protein Conformation Recombinant Proteins - chemistry Recombinant Proteins - metabolism Thermodynamics
Online-Zugang:	Volltext
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