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Phosphorylation of Initiation Factor eIF-2 and Ribosomal Protein S6 and the Regulation of Mammalian Protein Synthesis

  • Odd Nygård
  • Peter Westermann
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  • 62 Downloads

Abstract

The reversible phosphorylation of eIF-2 and of protein S6 is implicated in the regulation of protein synthesis in several eukaryotic cell types. In the case of eIF-2 it has been shown that phosphorylation impairs the ability of the factor to exchange bound GDP for GTP. This reaction is catalysed by a high molecular weight protein complex, the interaction of which with eIF-2 is modulated by phosphorylation of the latter. GDP is generated by hydrolysis of GTP during 80S initiation complex formation, and also prematurely during 40S complex formation (at least in vitro). Since it must be exchanged for GTP before eIF-2 can function catalytically, phosphorylation impairs the ability of eIF-2 to recycle between successive rounds of protein synthesis.

Keywords

Ribosomal Protein Guanine Nucleotide Exchange Factor Initiation Complex Amino Acid Starvation Isotonic Condition 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© The Human Press Inc. 1983

Authors and Affiliations

  • Odd Nygård
    • 1
  • Peter Westermann
    • 2
  1. 1.The Wenner-Gren InstituteUniversity of StockholmStockholmSweden
  2. 2.Central Institute of Molecular BiologyAcademy of Sciences of GDRBerlin-BuchGermany

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