The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1

• Published in: Nature structural & molecular biology Vol. 12; no. 6; pp. 497 - 504
• Main Authors: Craig, Elizabeth A, Huang, Peggy, Gautschi, Matthias, Walter, William, Rospert, Sabine
• Format: Journal Article
• Language: English
• Published: United States Nature Publishing Group 01.06.2005
• Subjects: Adenosine Triphosphatases - metabolism; Adenosine Triphosphate - metabolism; Amino acids; ATP; DNA binding proteins; DNA-Binding Proteins - physiology; HSP70 Heat-Shock Proteins - chemistry; HSP70 Heat-Shock Proteins - genetics; HSP70 Heat-Shock Proteins - metabolism; HSP70 Heat-Shock Proteins - physiology; Hydrolysis; Kinetics; Models, Molecular; Molecular Chaperones; Phenotype; Physiological aspects; Polypeptides; Protein Conformation; Proteins; Ribonucleic acid; Ribosomes; Ribosomes - metabolism; RNA; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Saccharomyces cerevisiae Proteins - physiology; Structure; Yeast; Yeasts; United States
• ISSN: 1545-9993; 1545-9985
• DOI: 10.1038/nsmb942

J-proteins are obligate partners of Hsp70s, forming a ubiquitous class of molecular chaperone machinery. The ribosome-associated Hsp70 of yeast Ssb binds nascent polypeptides as they exit the ribosome. Here we report that the ribosome-associated J-protein Zuo1 is the partner of Ssb. However, Zuo1 efficiently stimulates the ATPase activity of Ssb only when in complex with another Hsp70, Ssz1. Ssz1 binds ATP, but none of the 11 different amino acid substitutions in the ATP-binding cleft affected Ssz1 function in vivo, suggesting that neither nucleotide binding nor hydrolysis is required. We propose that Ssz1's predominant function in the cell is to facilitate Zuo1's ability to function as a J-protein partner of Ssb on the ribosome, serving as an example of an Hsp70 family member that has evolved to carry out functions distinct from that of a chaperone.