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PMID: 1570324 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Anticodon-independent aminoacylation of an RNA minihelix with valine.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 89 ·No. 9 ·1992-05-01 ·Pages 3990-4

Frugier M, Florentz C, Giegé R

Abstract

Minihelices mimicking the amino acid acceptor and anticodon branches of yeast tRNA(Val) have been synthesized by in vitro transcription of synthetic templates. It is shown that a minihelix corresponding to the amino acid acceptor branch and containing solely a valine-specific identity nucleotide can be aminoacylated by yeast valyl-tRNA synthetase. Its charging ability is lost after mutating this nucleotide. This ability is stimulated somewhat by the addition of a second hairpin helix that mimicks the anticodon arm, which suggests that information originating from the anticodon stem-loop can be transmitted to the active site of the enzyme by the core of the protein.

MeSH Terms
Anticodon Base Sequence Hydrogen Bonding In Vitro Techniques Molecular Sequence Data RNA, Transfer, Val/chemistry,metabolism Saccharomyces cerevisiae Structure-Activity Relationship Transfer RNA Aminoacylation Valine-tRNA Ligase/metabolism
Chemicals
Anticodon RNA, Transfer, Val Valine-tRNA Ligase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Frugier M
Laboratoire de Biochimie, Centre National de la Recherche Scientifique, Strasbourg, France.
Florentz C
Giegé R
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35 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.89.9.3990
Published
1992-05-01
Pages
3990-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC525617
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.89.9.3990 PMC Full Text View journal details
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