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Originally published In Press as doi:10.1074/jbc.M100266200 on January 22, 2001

J. Biol. Chem., Vol. 276, Issue 17, 14426-14433, April 27, 2001
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The Yeast hsp70 Homologue Ssa Is Required for Translation and Interacts with Sis1 and Pab1 on Translating Ribosomes*

Lynn E. HortonDagger , Philip James§, Elizabeth A. Craig§, and Jack O. Hensold||

From the Department of Medicine, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106, the  Department of Medicine, University Hospitals of Cleveland and The Cleveland Veteran's Affairs Medical Center, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106, and the § Department of Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin 53706

The 70-kDa heat shock proteins are molecular chaperones that participate in a variety of cellular functions. This chaperone function is stimulated by interaction with hsp40 proteins. The Saccharomyces cerevisiae gene encoding the essential hsp40 homologue, SIS1, appears to function in translation initiation. Mutations in ribosomal protein L39 (rpl39) complement loss-of-function mutations in SIS1 as well as PAB1 (poly(A)-binding protein), suggesting a functional interaction between these proteins. However, while a direct interaction between Sis1 and Pab1 is not detectable, both of these proteins physically interact with the essential Ssa (and not Ssb) family of hsp70 proteins. This interaction is mediated by the variable C-terminal domain of Ssa. Subcellular fractionations demonstrate that the binding of Ssa to ribosomes is dependent upon its C terminus and that its interaction with Sis1 and Pab1 occurs preferentially on translating ribosomes. Consistent with a function in translation, depletion of Ssa protein produces a general translational defect that appears similar to loss of Sis1 and Pab1 function. This translational effect of Ssa appears mediated, at least in part, by its affect on the interaction of Pab1 with the translation initiation factor, eIF4G, which is dramatically reduced in the absence of functional Ssa protein.

* This work was supported in part by a grant from the American Cancer Society, Cuyahoga Unit (to J. O. H.) and by National Institutes of Health Grant RO1 GM31107 (to E. A. C.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by National Institutes of Health Grants HK07147-21A1 and DK09915.

|| To whom correspondence should be addressed: Dept. of Hematology and Oncology, 10900 Euclid Ave., BRB309B, Cleveland, OH 44106-4937. Tel.: 216-368-8758; Fax: 216-368-1166; E-mail: joh2@po.cwru.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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