NDLI: Misactivated amino acids translocate at similar rates across surface of a tRNA synthetase.

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Misactivated amino acids translocate at similar rates across surface of a tRNA synthetase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nomanbhoy, T. K. Schimmel, P. R.
Description	Author Affiliation: Nomanbhoy TK ( The Skaggs Institute for Chemical Biology, The Scripps Research Institute, Beckman Center, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.);
Abstract	Certain aminoacyl-tRNA synthetases have a second active site that destroys (by hydrolysis) errors of amino acid activation. For example, isoleucyl-tRNA synthetase misactivates valine (to produce valyl adenylate or Val-tRNA(Ile)) at its active site. The misactivated amino acid is then translocated to an editing site located >25 A away. The role of the misactivated amino acid in determining the rate of translocation is not known. Valyl-tRNA synthetase, a close homolog of isoleucyl-tRNA synthetase, misactivates threonine, alpha-aminobutyrate, and cysteine. In this paper, we use a recently developed fluorescence-energy-transfer assay to study translocation of misactivated threonine, alpha-aminobutyrate, and cysteine. Although their rates of misactivation are clearly distinct, their rates of translocation are similar. Thus, the rate of translocation is independent of the nature of the misactivated amino acid. This result suggests that the misactivated amino acid per se has little or no role in directing translocation.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	10
Volume Number	97
Language	English
Publisher	National Academy of Sciences
Publisher Date	2000-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acids Metabolism Valine-tRNA Ligase Chemistry Aminobutyrates Binding Sites Cloning, Molecular Cysteine Energy Transfer Escherichia Coli Enzymology Genetics Isoleucine-tRNA Ligase Kinetics Models, Molecular Open Reading Frames Protein Conformation RNA Editing RNA, Transfer, Val Recombinant Proteins Spectrometry, Fluorescence Threonine Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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