Histidine 66 in Escherichia coli elongation factor Tu selectively stabilizes aminoacyl-tRNAs

Stephen J. Chapman, Jared M. Schrader, Olke C. Uhlenbeck*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

The universally conserved His-66 of elongation factor Tu (EFTu) stacks on the side chain of the esterified Phe of Phe-tRNA Phe. The affinities of eight aminoacyl-tRNAs were differentially destabilized by the introduction of the H66A mutation into Escherichia coli EF-Tu, whereas Ala-tRNA Ala and Gly-tRNA Gly were unaffected. The H66F and H66W proteins each show a different pattern of binding of 10 different aminoacyltRNAs, clearly showing that this position is critical in establishing the specificity of EF-Tu for different esterified amino acids. However, the H66A mutation does not greatly affect the ability of the ternary complex to bind ribosomes, hydrolyze GTP, or form dipeptide, suggesting that this residue does not directly participate in ribosomal decoding. Selective mutation of His-66 may improve the ability of certain unnatural amino acids to be incorporated by the ribosome.

Original languageEnglish (US)
Pages (from-to)1229-1234
Number of pages6
JournalJournal of Biological Chemistry
Volume287
Issue number2
DOIs
StatePublished - Jan 6 2012

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Histidine 66 in Escherichia coli elongation factor Tu selectively stabilizes aminoacyl-tRNAs'. Together they form a unique fingerprint.

Cite this