skip to main content
Dunkle Research Group
  • Home
  • Research
  • People
  • Pubs
  • News
  • Contact
  • Pics
  • Structures

New Dunkle group publication in JBC on similarities between ErmC and ErmE

12/18/2020

 
Picture
Erythromycin resistance methyltransferase (Erm) enzymes are a clinically important mechanism of multi-drug antibiotic resistance rendering bacteria resistant to macrolide, lincosamide and ketolide antibiotics. Whether or not all Erm enzymes bind to their rRNA substrate in a similar manner is an outstanding question. A new publication from the Dunkle group titled "Shared requirements for key residues in the antibiotic resistance enzymes ErmC and ErmE suggest a common mode of RNA recognition" appeared in the December 18 edition of the Journal of Biological Chemistry. The article demonstrates that similar conserved residues in ErmC or ErmE are required for function by deploying in vivo and in vitro assays on a collection of site-directed mutants. Also a structural model for how Erm enzymes bind rRNA is presented.

Comments are closed.

    Archives

    May 2022
    December 2020
    November 2019
    June 2019
    May 2019
    October 2018
    June 2018
    March 2018
    February 2018
    January 2018
    August 2017
    June 2017
    April 2017
    March 2017
    February 2017
    December 2016
    November 2016

    Categories

    All

    RSS Feed

Picture
Accessibility | Equal Opportunity | UA Disclaimer | Site Disclaimer | Privacy | Copyright © 2020
The University of Alabama | Tuscaloosa, AL 35487 | (205) 348-6010
Website provided by the Center for Instructional Technology, Office of Information Technology
  • Home
  • Research
  • People
  • Pubs
  • News
  • Contact
  • Pics
  • Structures