Title

At the confluence of ribosomally synthesized peptide modification and radical

Digital Object Identifier / DOI

https://doi.org/10.1074/jbc.r117.797399

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.

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