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PMID: 1472058 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Escherichia coli tRNA(Asp) recognition mechanism differing from that of the yeast system.

Biochemical and biophysical research communications ·Vol. 189 ·No. 2 ·1992-12-15 ·Pages 856-62

Nameki N, Tamura K, Himeno H, Asahara H, Hasegawa T, Shimizu M

Abstract

Various tRNA transcripts were constructed to study the identity elements of Escherichia coli tRNA(Asp). Base substitutions from G34 to U34 at the first position of the anticodon, and from U35 to A35 at the second, severely impaired the aspartate charging activity. The activity was also decreased, but in a more moderate fashion, by base changes at G2-C71, C36 and C38. Identity nucleotides of tRNA(Asp) are distributed in a different fashion between E. coli and yeast, which occur at the second base pair of the acceptor stem, G10-U25 base pair in the D-stem and 3' half of the anticodon loop.

MeSH Terms
Anticodon Base Sequence Escherichia coli/metabolism Kinetics Models, Structural Molecular Sequence Data Nucleic Acid Conformation RNA, Transfer, Asn/chemistry,genetics RNA, Transfer, Asp/chemistry,genetics,metabolism RNA, Transfer, Val/chemistry,genetics Saccharomyces cerevisiae/metabolism Transcription, Genetic
Chemicals
Anticodon RNA, Transfer, Asn RNA, Transfer, Asp RNA, Transfer, Val
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Nameki N
Institute of Space and Astronautical Science, Kanagawa, Japan.
Tamura K
Himeno H
Asahara H
Hasegawa T
Shimizu M
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1992-12-15
Pages
856-62
Language
English
Region
United States
NLM ID
0372516
Subset
IM
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