NDLI: Enzymatic aminoacylation of an eight-base-pair microhelix with histidine.

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Enzymatic aminoacylation of an eight-base-pair microhelix with histidine.

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Enzymatic aminoacylation of an eight-base-pair microhelix with histidine.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Schimmel, P. Francklyn, C.
Description	Author Affiliation: Francklyn C ( Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.);
Abstract	The major determinant for the identity of alanine tRNAs is a single base pair in the acceptor helix that is proximal to the site of amino acid attachment. A 7-base-pair microhelix that recreates the acceptor helix can be charged with alanine. No other examples of charging of small helices with specific amino acids have been reported, to our knowledge. We show here that a 13-base-pair and an 8-base-pair hairpin helix that reconstruct a domain and subdomain, respectively, of histidine tRNAs can be charged with histidine. We also show that transplantation of a base pair that is unique to histidine tRNAs is sufficient to consider histidine acceptance on a domain and subdomain of alanine tRNA. Both alanine and histidine aminoacyl-tRNA synthetases retain specificity for their cognate synthetic substrates. Alanine- and histidine-specific microhelices may resemble a system that arose early in the evolution of charging and coding.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	87
Language	English
Publisher	National Academy of Sciences
Publisher Date	1990-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Alanine-tRNA Ligase Metabolism Histidine-tRNA Ligase RNA, Transfer, His Base Composition Kinetics Models, Molecular Molecular Sequence Data Nucleic Acid Conformation RNA, Transfer, Ala Genetics Substrate Specificity Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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