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PMID: 6340062 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Structural investigation of Phe-tRNAPhe from E.coli bound to the ribosomal A-site.

Nucleic acids research ·Vol. 11 ·No. 3 ·1983-02-11 ·Pages 575-89

Bertram S, Göringer U, Wagner R

Abstract

Kethoxal modification of guanosines within Phe-tRNAPhe from E. coli was studied for tRNA in the free state and specifically bound to the ribosomal A-site. Complex formation with the ribosome results in a protection from chemical modification of two distant sites in the tRNA molecule. The guanosines affected are G-18 and G-19, located in the D-loop, and G-34 in the anticodon loop. Modification of Phe-tRNAPhe in the absence of ribosomes leads to a destabilisation of the tRNA structure. Our data are consistent with the conclusion that modification of G-34 at the anticodon loop triggers a conformational instability in distant parts of the tRNA molecule.

MeSH Terms
Aldehydes/pharmacology Antiviral Agents/pharmacology Base Sequence Butanones Escherichia coli/genetics,metabolism Kinetics RNA, Transfer, Amino Acyl/genetics Ribosomes/drug effects,metabolism
Chemicals
Aldehydes Antiviral Agents Butanones RNA, Transfer, Amino Acyl kethoxal
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bertram S
Göringer U
Wagner R
References (11)
11 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1983-02-11
Pages
575-89
Language
English
Region
England
NLM ID
0411011
PMCID
PMC325738
Subset
IM
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