| First Author | Quevillon S | Year | 1996 |
| Journal | FEBS Lett | Volume | 395 |
| Issue | 1 | Pages | 63-7 |
| PubMed ID | 8849690 | Mgi Jnum | J:113818 |
| Mgi Id | MGI:3687699 | Doi | 10.1016/0014-5793(96)01005-8 |
| Citation | Quevillon S, et al. (1996) The p18 component of the multisynthetase complex shares a protein motif with the beta and gamma subunits of eukaryotic elongation factor 1. FEBS Lett 395(1):63-7 |
| abstractText | 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. |
