NDLI: Modulation of tRNAAla identity by inorganic pyrophosphatase.

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Modulation of tRNAAla identity by inorganic pyrophosphatase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wolfson, Alexey D. Uhlenbeck, Olke C.
Description	Author Affiliation: Wolfson AD ( Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309-0215, USA.);
Abstract	A highly sensitive assay of tRNA aminoacylation was developed that directly measures the fraction of aminoacylated tRNA by following amino acid attachment to the 3'-(32)P-labeled tRNA. When applied to Escherichia coli alanyl-tRNA synthetase, the assay allowed accurate measurement of aminoacylation of the most deleterious mutants of tRNA(Ala). The effect of tRNA(Ala) identity mutations on both aminoacylation efficiency (k(cat)/K(M)) and steady-state level of aminoacyl-tRNA was evaluated in the absence and presence of inorganic pyrophosphatase and elongation factor Tu. Significant levels of aminoacylation were achieved for tRNA mutants even when the k(cat)/K(M) value is reduced by as much as several thousandfold. These results partially reconcile the discrepancy between in vivo and in vitro analysis of tRNA(Ala) identity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Pyrophosphatases Metabolism RNA, Transfer, Ala Escherichia Coli Enzymology Inorganic Pyrophosphatase Kinetics Mutation Peptide Elongation Factor Tu Plasmids Protein Binding Protein Biosynthesis Time Factors Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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