eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation

Martin D. Jennings and Graham D. Pavitt ()
Additional contact information
Martin D. Jennings: Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK
Graham D. Pavitt: Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK

Nature, 2010, vol. 465, issue 7296, 378-381

Abstract: Translation initiation by eIF2 The translation factor that helps deliver the initiator tRNA to the ribosome, eIF2, uses the energy of GTP hydrolysis for function. Another factor, eIF5, was known to accelerate the GTPase activity of eIF2 when it was bound to the initiator tRNA and the ribosome. In this study two other roles for eIF5 have been defined. One involves stabilizing the binding of GDP, the product of GTP hydrolysis, to eIF2. The other involves its acting with phosphorylated eIF2 to inhibit the guanine nucleotide exchange factor, eIF2B. These results clarify our understanding of how translation initiation is regulated.

Date: 2010
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature09003 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:465:y:2010:i:7296:d:10.1038_nature09003

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature09003

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().