The p18 component of the multisynthetase complex shares a protein motif with the β and γ subunits of eukaryotic elongation factor 1
- 14 October 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 395 (1), 63-67
- https://doi.org/10.1016/0014-5793(96)01005-8
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 β and γ 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.Keywords
This publication has 21 references indexed in Scilit:
- Valyl‐tRNA Synthetase from ArtemiaEuropean Journal of Biochemistry, 1995
- The cytoskeleton and mRNA localizationCurrent Opinion in Cell Biology, 1992
- Mammalian prolyl-tRNA synthetase corresponds to the ≈ 150 kDa subunit of the high-Mr aminoacyl-tRNA synthetase complexBiochimie, 1992
- Purification and properties of a high‐molecular‐mass complex between Val‐tRNA synthetase and the heavy form of elongation factor 1 from mammalian cellsEuropean Journal of Biochemistry, 1991
- Co-purification of the aminoacyl-tRNA synthetase complex with the elongation factor eEF1Biochemical and Biophysical Research Communications, 1991
- Basic local alignment search toolJournal of Molecular Biology, 1990
- Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloningBiochemistry, 1987
- Association of an aminoacyl-tRNA synthetase complex and of phenylalanyl-tRNA synthetase with the cytoskeletal framework fraction from mammalian cellsExperimental Cell Research, 1985
- Association of methionyl-tRNA synthetase with detergent-insoluble components of the rough endoplasmic reticulum.The Journal of cell biology, 1983
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970