The N terminus of eukaryotic translation elongation factor 3 interacts with 18 S rRNA and 80 S ribosomes.

The Journal of Biological Chemistry
R R GontarekC D Prescott

Abstract

Elongation factor-3 (EF-3) is an essential fungal-specific translation factor which exhibits a strong ribosome-dependent ATPase activity and has sequence homologies that may predict domains critical for its role in protein synthesis, including a domain at the N terminus, which exhibits sequence homology with Escherichia coli ribosomal protein S5. A portion of the N terminus of Saccharomyces cerevisiae EF-3 (spanning the S5 homology region) has been cloned, expressed, and purified from E. coli. UV cross-linking experiments revealed that the N-terminal EF-3 protein (N-term EF-3) can be specifically cross-linked to 18 S rRNA. Filter-binding assays confirmed these data, and also established that the interaction has a Kd approximately 238 nM. Additional evidence shows that N-term EF-3 is able to associate with yeast ribosomes and inhibit the ribosome-dependent ATPase activity of native EF-3. These data taken together suggest that at least one of the ribosome-binding sites of EF-3 is located at the N terminus.

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Citations

Jun 26, 2001·Research in Microbiology·K Chakraburtty
Apr 27, 1999·The International Journal of Biochemistry & Cell Biology·K Chakraburtty
Aug 14, 2012·The Journal of Biological Chemistry·Jyothsna VisweswaraiahEvelyn Sattlegger
Mar 13, 2001·Journal of Bacteriology·G BlakelyP R Williamson
Oct 12, 2000·Proceedings of the National Academy of Sciences of the United States of America·K Kimura, T Hirano
Aug 25, 2006·Nature·Christian B F AndersenRoland Beckmann
Dec 21, 2002·The Journal of Biological Chemistry·Monika AnandTerri Goss Kinzy
Apr 5, 2000·The Journal of Biological Chemistry·R KambampatiK Chakraburtty

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