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PMID: 347403 Published · ppublish English Journal Article

The effect of specific structural modification on the biological activity of E. coli arginine tRNA.

Nucleic acids research ·Vol. 5 ·No. 3 ·1978-03-00 ·Pages 879-92

Kruse TA, Clark BF

Abstract

Escherichia coli arginine tRNA1 has been modified at position s2C32 with iodoacetamide and a spin labelled derivative. The small effects on the charging ability of tRNA by the modifiications suggest that the synthetase does not bind to the tRNA in this region of the anticodon loop before the anticodon. A ternary complex of elongation factor Tu, GTP and the modified Arg-tRNA, can be formed allowing future studies of enzymatic binding to the ribosome. Using the triplet binding assay the native Arg-tRNA1 decodes all 4 codons beginning with CG. The modified Arg-tRNA1 has a restricted decoding but the decoding pattern is still unusual according to the Wobble Hypothesis.

MeSH Terms
Amino Acyl-tRNA Synthetases/metabolism Anticodon Arginine Arginine-tRNA Ligase/metabolism Codon Escherichia coli Guanylyl Imidodiphosphate/metabolism Peptide Elongation Factors RNA, Bacterial/metabolism RNA, Transfer/metabolism Ribosomes/metabolism Spin Labels Structure-Activity Relationship
Chemicals
Anticodon Codon Peptide Elongation Factors RNA, Bacterial Spin Labels Guanylyl Imidodiphosphate RNA, Transfer Arginine Amino Acyl-tRNA Synthetases Arginine-tRNA Ligase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kruse T A
Clark B F
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21 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/5.3.879
Published
1978-03-00
Pages
879-92
Language
English
Region
England
NLM ID
0411011
PMCID
PMC342030
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/5.3.879 PMC Full Text View journal details
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