Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro

Biochem Biophys Res Commun. 2008 Jan 25;365(4):718-23. doi: 10.1016/j.bbrc.2007.11.028.

Catherine M Guzzo ¹, David C H Yang

Affiliations

Affiliation

1 Department of Chemistry, Georgetown University, Washington, DC 20057, USA.

PMID: 18029264 DOI: 10.1016/j.bbrc.2007.11.028

Abstract

The functions of evolved mammalian supramolecular assemblies and extensions of enzymes are not well understood. Human lysyl-tRNA synthetase (hKRS) only upon the removal of the amino-terminal extension (hKRSDelta60) bound to EF1alpha and was stimulated by EF1alphain vitro. HKRS and hKRSDelta60 were also differentially stimulated by aspartyl-tRNA synthetase (AspRS) from the multi-synthetase complex. The non-synthetase protein from the multi-synthetase complex p38 alone did not affect hKRS lysylation but inhibited the AspRS-mediated stimulation of hKRS. These results revealed the functional interactions of hKRS and shed new lights on the functional significance of the structural evolution of multienzyme complexes and appended extensions.

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