Conformational alteration of protein synthesis elongation factor EF-Tu by EF-Ts and by kirromycin. Journal Article uri icon



  • Alterations of the structure of EF-Tu have been investigated by using the rate of EF-Tu cleavage by trypsin as a conformational probe. The presence of EF-Ts bound to EF-Tu results in a 10-fold increase in the cleavage rate. The antibiotic kirromycin, which inhibits protein synthesis by virtue of its interaction with EF-Tu, mimics this effect of EF-Ts. Both kirromycin and EF-Ts also facilitate the exchange of free GDP with GDP bound to EF-Tu. The results suggest that EF-Ts and kirromycin induce a similar conformational change in EF-Tu, thereby "opening" the guanine nucleotide binding site. The trypsin-cleaved EF-Tu still can bind GDP and EF-Ts and can function in Qbeta replicase, but it no longer spontaneously renatures following denaturation in urea.

publication date

  • August 1, 1977

has restriction

  • green

Date in CU Experts

  • April 22, 2014 11:29 AM

Full Author List

  • Blumenthal T; Douglass J; Smith D

author count

  • 3

Other Profiles

International Standard Serial Number (ISSN)

  • 0027-8424

Electronic International Standard Serial Number (EISSN)

  • 1091-6490

Additional Document Info

start page

  • 3264

end page

  • 3267


  • 74


  • 8