Domain and nucleotide dependence of the interaction between Saccharomyces cerevisiae translation elongation factors 3 and 1A

Monika Anand, Barvhi Balar, Rory Ulloque, Stephane R. Gross, Terri G. Kinzy

Research output: Contribution to journalArticle

Abstract

Eukaryotic translation elongation factor 3 (eEF3) is a fungal-specific ATPase proposed to catalyze the release of deacylated-tRNA from the ribosomal E-site. In addition, it has been shown to interact with the aminoacyl-tRNA binding GTPase elongation factor 1A (eEF1A), perhaps linking the E and A sites. Domain mapping demonstrates that amino acids 775-980 contain the eEF1A binding sites. Domain III of eEF1A, which is also involved in actin-related functions, is the site of eEF3 binding. The binding of eEF3 to eEF1A is enhanced by ADP, indicating the interaction is favored post-ATP hydrolysis but is not dependent on the eEF1A-bound nucleotide. A temperature-sensitive P915L mutant in the eEF1A binding site of eEF3 has reduced ATPase activity and affinity for eEF1A. These results support the model that upon ATP hydrolysis, eEF3 interacts with eEF1A to help catalyze the delivery of aminoacyl-tRNA at the A-site of the ribosome. The dynamics of when eEF3 interacts with eEF1A may be part of the signal for transition of the post to pre-translocational ribosomal state in yeast.
Original languageEnglish
Pages (from-to)32318-32326
Number of pages9
JournalJournal of Biological Chemistry
Volume281
DOIs
Publication statusPublished - 27 Oct 2006

Bibliographical note

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

Keywords

  • eukaryotic translation elongation factor 3
  • deacylated-tRNA
  • E-site
  • aminoacyl-tRNA binding GTPase elongation factor 1A
  • eEF1A
  • A sites
  • amino acids 775-980
  • eEF3 binding
  • ADP
  • post-ATP hydrolysis
  • eEF1A-bound nucleotide
  • P915L
  • ATPase activity
  • ATP hydrolysis
  • aminoacyl-tRNA
  • translocational ribosomal state
  • yeast

Fingerprint Dive into the research topics of 'Domain and nucleotide dependence of the interaction between Saccharomyces cerevisiae translation elongation factors 3 and 1A'. Together they form a unique fingerprint.

  • Cite this