a bacteriophage-encoded j-domain protein interacts with the dnakhsp70 chaperone and stabilizes the heat-shock factor σ32 of escherichia coli一个bacteriophage-encoded j-domain蛋白质与dnakhsp70交互伴侣蛋白和稳定的热休克因子σ32大肠杆菌.pdf

A Bacteriophage-Encoded J-Domain Protein Interacts with the DnaK/Hsp70 Chaperone and Stabilizes the Heat- Shock Factor s32 of Escherichia coli 1 1 2 2 2 Elsa Perrody , Anne-Marie Cirinesi , Carine Desplats , France Keppel , Franc¸oise Schwager , 3 2,4 1 Samuel Tranier , Costa Georgopoulos , Pierre Genevaux * ´ ´ ´ ´ 1 Laboratoire de Microbiologie et Genetique Moleculaire (LMGM), UMR5100, Centre National de la Recherche Scientifique (CNRS) and Universite Paul Sabatier, Toulouse, ´ ´ ´ ´ ` France, 2 Departement de Microbiologie et Medecine Moleculaire, CMU, Universite de Geneve, Geneva, Switzerland, 3 Institut de Pharmacologie et de Biologie Structurale, Centre National de la Recherche Scientifique (CNRS), Toulouse, France, 4 Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah, United States of America Abstract The universally conserved J-domain proteins (JDPs) are obligate cochaperone partners of the Hsp70 (DnaK) chaperone. They stimulate Hsp70’s ATPase activity, facilitate substrate delivery, and confer specific cellular localization to Hsp70. In this work, we have identified and characterized the first functional JDP protein encoded by a bacteriophage. Specifically, we show that the ORFan gene 057w of the T4-related enterobacteriophage RB43 encodes a bona fide JDP protein, named Rki, which specifically interacts with the Escherichia coli host multifunctional DnaK