Literature DB >> 6489525

Phosphorylation of elongation factor 1 in polyribosome fraction of rabbit reticulocytes.

E K Davydova, A S Sitikov, L P Ovchinnikov.   

Abstract

A single protein, Mr approximately 50000, is shown to be phosphorylated during incubation of a mono- and polyribosome fraction of rabbit reticulocytes with [gamma-32P]ATP at a low ionic strength. This protein has been identified as the elongation factor 1 alpha (EF-1 alpha). The phosphorylated EF-1 alpha, in contrast to the unmodified factor, is not detected in complexes with mono- and polyribosomes. It is suggested that the phosphorylation of EF-1 alpha can result in its decompartmentation from polyribosomes and thus affect the rate of protein synthesis.

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Year:  1984        PMID: 6489525     DOI: 10.1016/0014-5793(84)81206-5

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Elongation factor EF-1 alpha gene dosage alters translational fidelity in Saccharomyces cerevisiae.

Authors:  J M Song; S Picologlou; C M Grant; M Firoozan; M F Tuite; S Liebman
Journal:  Mol Cell Biol       Date:  1989-10       Impact factor: 4.272

Review 2.  Mechanism and regulation of eukaryotic protein synthesis.

Authors:  W C Merrick
Journal:  Microbiol Rev       Date:  1992-06

3.  The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and characterization of the protein.

Authors:  S Kahns; A Lund; P Kristensen; C R Knudsen; B F Clark; J Cavallius; W C Merrick
Journal:  Nucleic Acids Res       Date:  1998-04-15       Impact factor: 16.971

  3 in total

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