At the Confluence of Ribosomally Synthesized Peptide Modification and Radical S -adenosylmethionine (SAM) Enzymology
Iron–sulfur protein, Oxidation–reduction (redox), Peptide biosynthesis, Post-translational modification (PTM), Radical, RiPPs, SPASM, Radical SAM
College of Natual Science and Mathematics, Chemistry and Biochemistry
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.
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Latham, J. A., Barr, I., & Klinman, J. P. (2017). At the confluence of ribosomally synthesized peptide modification and radical S -adenosylmethionine (SAM) enzymology. The Journal of Biological Chemistry, 292(40), 16397-16405. DOI: 10.1074/jbc.r117.797399.