NDLI: The discriminator base influences tRNA structure at the end of the acceptor stem and possibly its interaction with proteins.

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The discriminator base influences tRNA structure at the end of the acceptor stem and possibly its interaction with proteins.

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The discriminator base influences tRNA structure at the end of the acceptor stem and possibly its interaction with proteins.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dyson, M. R. Rajbhandary, U. L. Mandal, N. Lee, C. P.
Description	Author Affiliation: Lee CP ( Department of Biology, Massachusetts Institute of Technology, Cambridge 02139-4307.);
Abstract	For many tRNAs, the discriminator base preceding the CCA sequence at the 3' end is important for aminoacylation. We show that the discriminator base influences the stability of the 1.72 base pair onto which it is stacked. Mutations of the discriminator base from adenosine to cytidine or uridine make the cytidine residue in the C1-G72 base pair of mutant Escherichia coli initiator tRNAs more reactive toward sodium bisulfite, the single-strand-specific reagent. The activity of the enzyme Met-tRNA transformylase toward these and other mutant initiator tRNAs is also consistent with destabilization of the 1.72 base pair in vitro and in vivo. By influencing the strength of the 1.72 base pair, the discriminator base could affect the energetic cost of opening the base pair and modulate the structure of the tRNA near the site of aminoacylation. For some aminoacyl-tRNA synthetases and other proteins that interact with tRNA, these factors could be important for specific recognition and/or formation of the transition state during catalysis.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	90
Language	English
Publisher	National Academy of Sciences
Publisher Date	1993-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hydroxymethyl And Formyl Transferases RNA, Transfer, Met Chemistry Acyltransferases Metabolism Hydrogen Bonding Kinetics Methionine-tRNA Ligase Molecular Sequence Data Mutagenesis, Site-Directed Nucleic Acid Conformation Protein Binding Ribonucleoproteins Structure-Activity Relationship Transfer RNA Aminoacylation Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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