Skip to main content
eScholarship
Open Access Publications from the University of California

At the confluence of ribosomally synthesized peptide modification and radical S-adenosylmethionine (SAM) enzymology.

  • Author(s): Latham, John A
  • Barr, Ian
  • Klinman, Judith P
  • et al.

Published Web Location

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5633103/
No data is associated with this publication.
Abstract

Radical S-adenosylmethionine (RS) enzymology has emerged as a major biochemical strategy for the homolytic cleavage of unactivated C-H bonds. At the same time, the post-translational modification of ribosomally synthesized peptides is a rapidly expanding area of investigation. We discuss the functional cross-section of these two disciplines, highlighting the recently uncovered importance of protein-protein interactions, especially between the peptide substrate and its chaperone, which functions either as a stand-alone protein or as an N-terminal fusion to the respective RS enzyme. The need for further work on this class of enzymes is emphasized, given the poorly understood roles performed by multiple, auxiliary iron-sulfur clusters and the paucity of protein X-ray structural data.

Many UC-authored scholarly publications are freely available on this site because of the UC Academic Senate's Open Access Policy. Let us know how this access is important for you.

Item not freely available? Link broken?
Report a problem accessing this item