Format

Send to

Choose Destination
J Biol Chem. 2012 Jan 6;287(2):1229-34. doi: 10.1074/jbc.M111.294850. Epub 2011 Nov 21.

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

Author information

1
Department of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA.

Abstract

The universally conserved His-66 of elongation factor Tu (EF-Tu) 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 aminoacyl-tRNAs, 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.

PMID:
22105070
PMCID:
PMC3256880
DOI:
10.1074/jbc.M111.294850
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center