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. 1974 Feb;1(2):217–221. doi: 10.1093/nar/1.2.217

The role of the anticodon in the interaction between methionyl-tRNA synthetase and bacterial initiator tRNA?

CJ Bruton 1, BFC Clark 1
PMCID: PMC343340  PMID: 4607244

Abstract

Complementary and antiparallel oligonucleotides bind to exposed regions of the tRNA molecule. Aminoacylation in the presence of triplets has been used to determine the role of the anticodon in the interaction between methionyl-tRNA synthetase and initiator tRNA. ApUpG has no effect on the charging even when 70% of the tRNA is bound to the triplet, whereas in the presence of GpGpU which binds to the A-C-C sequence adjacent to the 3′ terminal adenosine that fraction of the tRNA which is bound to the triplet is completely unavailable for charging. Hence the anticodon is probably not involved in a primary interaction while the A-C-C-A-OH clearly is. This conclusion is supported by the failure of the isolated anticodon loop and stem oligonucleotides to inhibit the aminoacylation reaction.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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