At the confluence of ribosomally synthesized peptide modification and radical
Department
Natural Sciences and Mathematics
Document Type
Article
Source
Journal of Biochemistry
Publication Date
10-6-2017
ISSN
1083-351X
Volume
292
Issue
40
First Page
16397
Last Page
16405
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.
PubMed ID
28830931
Rights
© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.