The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1.

Abstract:

:In higher eukaryotes, nine aminoacyl-tRNA synthetases form a multienzyme complex also comprising the three auxiliary proteins p18, p38 and p43, of apparent molecular masses of 18, 38 and 43 kDa. The function of these proteins, invariably found associated to the synthetase components of the complex, is unknown. In order to gain a more precise view of the structural and functional organization of this complex, we cloned the cDNA encoding the p18 component. The 174-amino-acid hamster protein displays sequence homology with the NH2-terminal moieties of the beta and gamma subunits of the elongation factor EF-1H, implicated in subunits interaction. The homologous polypeptide fragment of about 90 amino acids is also recovered in the NH2-terminal extension of human valyl-tRNA synthetase, involved in its assembly with EF-1H. These results suggest that p18 contributes a template for association of the multisynthetase complex with EF-1H.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Quevillon S,Mirande M

doi

10.1016/0014-5793(96)01005-8

subject

Has Abstract

pub_date

1996-10-14 00:00:00

pages

63-7

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(96)01005-8

journal_volume

395

pub_type

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