JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
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 PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Matts, R. L.
Right arrow Articles by London, I. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Matts, R. L.
Right arrow Articles by London, I. M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 259, Issue 11, 6708-6711, 06, 1984

The regulation of initiation of protein synthesis by phosphorylation of eIF-2(alpha) and the role of reversing factor in the recycling of eIF-2

RL Matts and IM London

The capacity of whole reticulocyte lysates to catalyze the dissociation of exogenously added eIF-2 X [3H]GDP was determined as a measure of their reversing factor (RF) activity in the recycling of eIF-2 for the maintenance or restoration of protein synthesis. We have examined the relationship of RF activity to the protein synthetic activity of the lysate under normal conditions and on inhibition of protein synthesis by heme deficiency, double-stranded RNA, or oxidized glutathione. A direct correlation was found between a lysate's capacity to synthesize protein and its ability to stimulate the dissociation of eIF-2 X GDP. These findings further support the proposed mechanism by which the phosphorylation of only 30-40% of the eIF-2(alpha) in the lysate renders the limiting amount of RF present non-functional, impairing the recycling of eIF-2 and thereby inhibiting the initiation of protein synthesis.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Appl. Physiol.Home page
F. Haddad, R. R. Roy, H. Zhong, V. R. Edgerton, and K. M. Baldwin
Atrophy responses to muscle inactivity. II. Molecular markers of protein deficits
J Appl Physiol, August 1, 2003; 95(2): 791 - 802.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
S. Uma, V. Thulasiraman, and R. L. Matts
Dual Role for Hsc70 in the Biogenesis and Regulation of the Heme-Regulated Kinase of the alpha Subunit of Eukaryotic Translation Initiation Factor 2
Mol. Cell. Biol., September 1, 1999; 19(9): 5861 - 5871.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1984 by the American Society for Biochemistry and Molecular Biology.