Structure of eEF3 and the mechanism of transfer RNA release from the E-site-Reference-Cited by-同舟云学术

Structure of eEF3 and the mechanism of transfer RNA release from the E-site

Published:2006-08-23 Issue:7112 Volume:443 Page:663-668
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Andersen Christian B. F.,Becker Thomas,Blau Michael,Anand Monika,Halic Mario,Balar Bharvi,Mielke Thorsten,Boesen Thomas,Pedersen Jan Skov,Spahn Christian M. T.,Kinzy Terri Goss,Andersen Gregers R.,Beckmann Roland

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature05126.pdf

Reference49 articles.

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2. Gontarek, R. R., Li, H., Nurse, K. & Prescott, C. D. The N terminus of eukaryotic translation elongation factor 3 interacts with 18S rRNA and 80S ribosomes. J. Biol. Chem. 273, 10249–10252 (1998)

3. Kambampati, R. et al. Limited proteolysis of yeast elongation factor 3. Sequence and location of the subdomains. J. Biol. Chem. 275, 16963–16968 (2000)

4. Triana-Alonso, F. J., Chakraburtty, K. & Nierhaus, K. H. The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor. J. Biol. Chem. 270, 20473–20478 (1995)

5. Kamath, A. & Chakraburtty, K. Role of yeast elongation factor 3 in the elongation cycle. J. Biol. Chem. 264, 15423–15428 (1989)

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