Exploring the specificity of bacterial elongation factor Tu for different tRNAs

Lee E. Sanderson, Olke C. Uhlenbeck*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

In order to identify amino acids in Thermus thermophilus elongation factor Tu which contribute to its specificity for different tRNAs, the binding affinities of 20 point mutations were compared to that of wild type protein using four tRNAs of differing affinities. The observed specificity for tRNA is the result of the varying contributions of five amino acids which make contacts with the T-stem and the 3′ terminus of tRNA. For three of the amino acids the test tRNAs differ in sequence at the site of contact, presumably explaining the specificity. However, the remaining two amino acids contact tRNA at conserved positions, suggesting that more global structural or dynamic properties of the free tRNA contribute to specificity.

Original languageEnglish (US)
Pages (from-to)6194-6200
Number of pages7
JournalBiochemistry
Volume46
Issue number21
DOIs
StatePublished - May 29 2007

ASJC Scopus subject areas

  • Biochemistry

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