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

Motorin YuA; A D Wolfson; A F Orlovsky; K L Gladilin

doi:10.1016/0014-5793(88)80492-7

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

FEBS Lett. 1988 Oct 10;238(2):262-4. doi: 10.1016/0014-5793(88)80492-7.

Authors

Motorin YuA¹, A D Wolfson, A F Orlovsky, K L Gladilin

Affiliation

¹ A.N. Bakh Institute of Biochemistry, Academy of Sciences of the USSR, Moscow.

PMID: 3169261
DOI: 10.1016/0014-5793(88)80492-7

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*

Substances

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