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Literature DB >> 3169261

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

A D Wolfson, A F Orlovsky, K L Gladilin.

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.

Entities: Gene Species

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Year: 1988 PMID： 3169261 DOI： 10.1016/0014-5793(88)80492-7

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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Cited

22 in total

1. A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII.

Authors: G T Sheu; J A Traugh
Journal: Mol Cell Biochem Date: 1999-01 Impact factor: 3.396

2. Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex.

Authors: S B Rho; M J Kim; J S Lee; W Seol; H Motegi; S Kim; K Shiba
Journal: Proc Natl Acad Sci U S A Date: 1999-04-13 Impact factor: 11.205

3. Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation.

Authors: J Sanders; J A Maassen; W Möller
Journal: Nucleic Acids Res Date: 1992-11-25 Impact factor: 16.971

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

1. A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CKII.

2. Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex.

3. Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation.

4. Channeling of aminoacyl-tRNA for protein synthesis in vivo.

5. A sequestered pool of aminoacyl-tRNA in mammalian cells.

Review 6. Mechanism and regulation of eukaryotic protein synthesis.

Review 7. Aminoacyl-tRNA synthetase complexes: molecular multitasking revealed.

8. Expression of human aspartyl-tRNA synthetase in COS cells.

9. Interaction between human tRNA synthetases involves repeated sequence elements.

10. Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the Cytoplasm of Human Cells.