Lysyl-tRNA synthetase interacts with EF1α, aspartyl-tRNA synthetase and p38 in vitro

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 (hKRSΔ60) bound to EF1α and was stimulated by EF1α in vitro. HKRS and hKRSΔ60 were also differentia...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2008-01, Vol.365 (4), p.718-723
Main Authors: Guzzo, Catherine M., Yang, David C.H.
Format: Article
Language:English
Subjects:
Amino-terminal extensions
Aminoacylation
EF1α
Enzyme interactions
Lysyl-tRNA synthetase
Multi-enzyme complex
p38
Supramolecular assembly
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Summary: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 (hKRSΔ60) bound to EF1α and was stimulated by EF1α in vitro. HKRS and hKRSΔ60 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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.11.028