Mammalian seryl-tRNA synthetase associates with mRNA in vivo and has homology to elongation factor 1α

A. Miseta, Charles L. Woodley, Jay R. Greenberg, Lawrence I. Slobin

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Previous work in our laboratories (Slobin, L. I., and Greenberg, J. R. (1988) Eur. J. Biochem. 173, 305-310) showed that messenger ribonucleoprotein (mRNP) particles possess a polypeptide component of approximately 62 kDa that appears to share a common epitope with eucaryotic elongation factor 1α (EF-1α). We report here that the previously unidentified mRNP constituent corresponds to seryl-tRNA synthetase (SerRS). Furthermore, we show that SerRS contains a sequence motif that is shared by both EF-1α and glutaminyl-tRNA synthetase. We also find that the association of SerRS with mRNA depends on the functional state of the latter. Our data suggest that SerRS may participate directly in the initiation phase of protein synthesis.

Original languageEnglish
Pages (from-to)19158-19161
Number of pages4
JournalJournal of Biological Chemistry
Volume266
Issue number29
Publication statusPublished - Oct 15 1991

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Serine-tRNA Ligase
Peptide Elongation Factor 1
Messenger RNA
glutaminyl-tRNA synthetase
Epitopes
Association reactions
Peptides
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Mammalian seryl-tRNA synthetase associates with mRNA in vivo and has homology to elongation factor 1α. / Miseta, A.; Woodley, Charles L.; Greenberg, Jay R.; Slobin, Lawrence I.

In: Journal of Biological Chemistry, Vol. 266, No. 29, 15.10.1991, p. 19158-19161.

Research output: Contribution to journalArticle

Miseta, A. ; Woodley, Charles L. ; Greenberg, Jay R. ; Slobin, Lawrence I. / Mammalian seryl-tRNA synthetase associates with mRNA in vivo and has homology to elongation factor 1α. In: Journal of Biological Chemistry. 1991 ; Vol. 266, No. 29. pp. 19158-19161.
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