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J. Biol. Chem., Vol. 278, Issue 9, 6985-6991, February 28, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/9/6985    most recent M209224200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Anand, M. Articles by Kinzy, T. G. Search for Related Content PubMed PubMed Citation Articles by Anand, M. Articles by Kinzy, T. G. Social Bookmarking                      What's this?

Functional Interactions between Yeast Translation Eukaryotic Elongation Factor (eEF) 1A and eEF3^*

Monika Anand, Kalpana Chakraburtty^§¶, Matthew J. Marton, Alan G. Hinnebusch, and Terri Goss Kinzy^**

From the  Department of Molecular Genetics, Microbiology & Immunology, University of Medicine and Dentistry of New Jersey Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, the ^§ Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 52226, and the  Laboratory of Gene Regulation and Development, NICHD, National Institutes of Health, Bethesda, Maryland 20892

The translation elongation machinery in fungi differs from other eukaryotes in its dependence upon eukaryotic elongation factor 3 (eEF3). eEF3 is essential in vivo and required for each cycle of the translation elongation process in vitro. Models predict eEF3 affects the delivery of cognate aminoacyl-tRNA, a function performed by eEF1A, by removing deacylated tRNA from the ribosomal Exit site. To dissect eEF3 function and its link to the A-site activities of eEF1A, we have identified a temperature-sensitive allele of the YEF3 gene. The F650S substitution, located between the two ATP binding cassettes, reduces both ribosome-dependent and intrinsic ATPase activities. In vivo this mutation increases sensitivity to aminoglycosidic drugs, causes a 50% reduction of total protein synthesis at permissive temperatures, slows run-off of polyribosomes, and reduces binding to eEF1A. Reciprocally, excess eEF3 confers synthetic slow growth, increased drug sensitivity, and reduced translation in an allele specific fashion with an E122K mutation in the GTP binding domain of eEF1A. In addition, this mutant form of eEF1A shows reduced binding of eEF3. Thus, optimal in vivo interactions between eEF3 and eEF1A are critical for protein synthesis.

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