HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Le, H. Articles by Gallie, D. R. Search for Related Content PubMed PubMed Citation Articles by Le, H. Articles by Gallie, D. R. Social Bookmarking                      What's this?

J Biol Chem, Vol. 273, Issue 32, 20084-20089, August 7, 1998

The Phosphorylation State of the Wheat Translation Initiation Factors eIF4B, eIF4A, and eIF2 Is Differentially Regulated during Seed Development and Germination

Hanh Le, Karen S. Browning^§, and Daniel R. Gallie

From the  Department of Biochemistry, University of California, Riverside, California 92521-0129 and the ^§ Department of Chemistry and Biochemistry and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712

The translation initiation factors (eIF) 4B and eIF2 are phosphoproteins whose phosphorylation state differs between mature seed and leaves. We examined the isoforms of eIF4B and the  and  subunits of eIF2 during the development and germination of wheat seed to determine whether the differences in their phosphorylation state are because of tissue-specific regulation or occur concomitant with changes in protein synthetic activity during development. eIF2 underwent phosphorylation through several intermediate isoforms that correlated with the increase and subsequent reduction in protein synthetic activity characteristic of seed development. eIF2 and eIF4B, present as highly phosphorylated isoforms during early seed development, underwent dephosphorylation during late development. eIF4B was rapidly phosphorylated within 20 h of germination, whereas eIF2 did not undergo dephosphorylation until 48-60 h of growth. A third factor, eIF4A, was predominantly nonphosphorylated throughout most of seed development and germination. These observations suggest that the phosphorylation state of eIF2, eIF2, and eIF4B is developmentally regulated in a way that correlates with the changes in protein synthetic activity but that some differences were also observed.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				K. Chibani, S. Ali-Rachedi, C. Job, D. Job, M. Jullien, and P. Grappin Proteomic Analysis of Seed Dormancy in Arabidopsis Plant Physiology, December 1, 2006; 142(4): 1493 - 1510. [Abstract] [Full Text] [PDF]

				I. M. Krab, C. Caldwell, D. R. Gallie, and J. F. Bol Coat protein enhances translational efficiency of Alfalfa mosaic virus RNAs and interacts with the eIF4G component of initiation factor eIF4F J. Gen. Virol., June 1, 2005; 86(6): 1841 - 1849. [Abstract] [Full Text] [PDF]

				F. van Breukelen, N. Sonenberg, and S. L. Martin Seasonal and state-dependent changes of eIF4E and 4E-BP1 during mammalian hibernation: implications for the control of translation during torpor Am J Physiol Regulatory Integrative Comp Physiol, August 1, 2004; 287(2): R349 - R353. [Abstract] [Full Text] [PDF]

				S. E. Dmitriev, I. M. Terenin, Y. E. Dunaevsky, W. C. Merrick, and I. N. Shatsky Assembly of 48S Translation Initiation Complexes from Purified Components with mRNAs That Have Some Base Pairing within Their 5' Untranslated Regions Mol. Cell. Biol., December 15, 2003; 23(24): 8925 - 8933. [Abstract] [Full Text] [PDF]

				H. Le, K. S. Browning, and D. R. Gallie The Phosphorylation State of Poly(A)-binding Protein Specifies Its Binding to Poly(A) RNA and Its Interaction with Eukaryotic Initiation Factor (eIF) 4F, eIFiso4F, and eIF4B J. Biol. Chem., June 2, 2000; 275(23): 17452 - 17462. [Abstract] [Full Text] [PDF]