Histidine 66 in Escherichia coli elongation factor tu selectively stabilizes aminoacyl-tRNAs. Journal Article uri icon

Overview

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.

publication date

  • January 1, 2012

has subject area

Date in CU Experts

  • March 13, 2015 12:56 PM

Full Author List

  • Chapman SJ; Schrader JM; Uhlenbeck OC

author count

  • 3

citation count

  • 3

Other Profiles

International Standard Serial Number (ISSN)

  • 0021-9258

Electronic International Standard Serial Number (EISSN)

  • 1083-351X

Additional Document Info

start page

  • 1229

end page

  • 1234

volume

  • 287

issue

  • 2