Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor.

FEBS letters ·Vol. 238 ·No. 2 ·1988-10-10 ·Pages 262-4

Motorin YuA, Wolfson AD, Orlovsky AF, Gladilin KL

Abstract

The high-molecular-mass form of valyl-tRNA synthetase is associated with the first elongation factor activity. It includes two polypeptides of about 50 kDa and two others of 40 and 30 kDa, identified as alpha, beta, gamma and delta subunits of eEF-1H. The complex of valyl-tRNA synthetase with eEF-1H is suggested to be a novel form of the first elongation factor.

MeSH Terms

Amino Acyl-tRNA Synthetases/metabolism Animals Chromatography, Gel Electrophoresis, Polyacrylamide Gel Molecular Weight Peptide Elongation Factor 1 Peptide Elongation Factors/metabolism Rabbits Valine-tRNA Ligase/metabolism

Chemicals

Peptide Elongation Factor 1 Peptide Elongation Factors peptide elongation factor 1H Amino Acyl-tRNA Synthetases Valine-tRNA Ligase

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Motorin YuA

A.N. Bakh Institute of Biochemistry, Academy of Sciences of the USSR, Moscow.

Wolfson A D

Orlovsky A F

Gladilin K L

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(88)80492-7

Published

1988-10-10

Pages

262-4

Language

English

Region

England

NLM ID

0155157

Subset

External Links

PubMed source DOI: 10.1016/0014-5793(88)80492-7 View journal details

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Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor.

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