Document Detail


eEF1A isoforms change in abundance and actin-binding activity during maize endosperm development.
MedLine Citation:
PMID:  14526107     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Eukaryotic elongation factor 1A (eEF1A) appears to be a multifunctional protein because several biochemical activities have been described for this protein, in addition to its role in protein synthesis. In maize (Zea mays) endosperm, the synthesis of eEF1A is increased in o2 (opaque2) mutants, and its concentration is highly correlated with the protein-bound lysine content. To understand the basis of this relationship, we purified eEF1A isoforms from developing endosperm and investigated their accumulation and their functional and structural properties. Formation of three isoforms appears to be developmentally regulated and independent of the o2 mutation, although one isoform predominated in one high lysine o2 inbred. The purified proteins differ in their ability to bind F-actin in vitro, suggesting that they are functionally distinct. However, they share similar aminoacyl-tRNA-binding activities. Tandem mass spectrometry revealed that each isoform is composed of the four same gene products, which are modified posttranslationally by methylation and phosphorylation. The chemical differences that account for their different actin-binding activities could not be determined.
Authors:
Jose A Lopez-Valenzuela; Bryan C Gibbon; Peter A Hughes; Theo W Dreher; Brian A Larkins
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2003-10-02
Journal Detail:
Title:  Plant physiology     Volume:  133     ISSN:  0032-0889     ISO Abbreviation:  Plant Physiol.     Publication Date:  2003 Nov 
Date Detail:
Created Date:  2003-11-12     Completed Date:  2004-03-24     Revised Date:  2013-06-09    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1285-95     Citation Subset:  IM    
Affiliation:
Department of Plant Sciences, University of Arizona, Tucson, Arizona 85721, USA.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism*
Amino Acid Sequence
Mass Spectrometry
Molecular Sequence Data
Mutation
Peptide Elongation Factor 1 / chemistry,  isolation & purification,  metabolism*
Protein Binding
Protein Isoforms / chemistry,  isolation & purification,  metabolism
RNA, Transfer, Amino Acyl / chemistry,  genetics,  metabolism
Seeds / growth & development*,  metabolism
Sequence Homology, Amino Acid
Zea mays / genetics,  growth & development*,  metabolism
Chemical
Reg. No./Substance:
0/Actins; 0/Peptide Elongation Factor 1; 0/Protein Isoforms; 0/RNA, Transfer, Amino Acyl
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