Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (171K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (12)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Monnier, A.
Right arrow Articles by Mulner-Lorillon, O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Monnier, A.
Right arrow Articles by Mulner-Lorillon, O.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2001, Vol. 29, No. 7 1453-1457
© 2001 Oxford University Press

Evidence for regulation of protein synthesis at the elongation step by CDK1/cyclin B phosphorylation

Annabelle Monnier, Robert Bellé*, Julia Morales, Patrick Cormier, Sandrine Boulben and Odile Mulner-Lorillon

Station Biologique de Roscoff, Université Pierre et Marie Curie (UFR 937), Centre National de la Recherche Scientifique (UPR 9042), Institut National des Sciences de l’Univers, BP 74, 29682 Roscoff Cedex, France

Eukaryotic elongation factor 1 (eEF-1) contains the guanine nucleotide exchange factor eEF-1B that loads the G protein eEF-1A with GTP after each cycle of elongation during protein synthesis. Two features of eEF-1B have not yet been elucidated: (i) the presence of the unique valyl-tRNA synthetase; (ii) the significance of target sites for the cell cycle protein kinase CDK1/cyclin B. The roles of these two features were addressed by elongation measurements in vitro using cell-free extracts. A poly(GUA) template RNA was generated to support both poly(valine) and poly(serine) synthesis and poly(phenylalanine) synthesis was driven by a poly(uridylic acid) template. Elongation rates were in the order phenylalanine > valine > serine. Addition of CDK1/cyclin B decreased the elongation rate for valine whereas the rate for serine and phenylalanine elongation was increased. This effect was correlated with phosphorylation of the eEF-1{delta} and eEF-1{gamma} subunits of eEF-1B. Our results demonstrate specific regulation of elongation by CDK1/cyclin B phosphorylation.

* To whom correspondence should be addressed. Tel: +33 2 98 29 23 46; Fax: +33 2 98 29 23 06; Email: belle{at}sb-roscoff.fr


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Cell. Biol.Home page
G. Sivan, N. Kedersha, and O. Elroy-Stein
Ribosomal Slowdown Mediates Translational Arrest during Cellular Division
Mol. Cell. Biol., October 1, 2007; 27(19): 6639 - 6646.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Z.-q. Chen, J. Dong, A. Ishimura, I. Daar, A. G. Hinnebusch, and M. Dean
The Essential Vertebrate ABCE1 Protein Interacts with Eukaryotic Initiation Factors
J. Biol. Chem., March 17, 2006; 281(11): 7452 - 7457.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Vanwetswinkel, J. Kriek, G. R. Andersen, P. Guntert, J. Dijk, G. W. Canters, and G. Siegal
Solution Structure of the 162 Residue C-terminal Domain of Human Elongation Factor 1B{gamma}
J. Biol. Chem., October 31, 2003; 278(44): 43443 - 43451.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.