Mycofactocin biosynthesis: modification of the peptide MftA by the radical S‐adenosylmethionine protein MftC1. Issue 16 (29th June 2016)

• Record Type: Journal Article
• Authors: Khaliullin, Bulat; Aggarwal, Priyanka; Bubas, Michael; Eaton, Gareth R.; Eaton, Sandra S.; Latham, John A.
• Is Part Of: FEBS letters. Volume 590:Issue 16(2016)
• Page Start: 2538
• Page End: 2548
• Publication Date: 2016-06-29
• Subjects: mycofactocin -- peptide interaction -- radical S‐adenosylmethionine; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12249
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Mycofactocin is a putative, peptide derived, cofactor that is associated primarily with the Mycobacterium genera including the pathogen M. tuberculosis . The pathway consists of the three genes mftA, mftB, and mftC that encode for the peptide substrate, peptide chaperone, and a radical S‐adenosylmethionine protein (RS), respectively. Here, we show that the MftB acts as a peptide chaperone, binding MftA with a submicromolar K D (~ 100 nm ) and MftC with a low micromolar K D (~ 2 μm ). Moreover, we demonstrate that MftC is a radical S‐adenosylmethionine (SAM) enzyme. Finally, we show that MftC catalyzes the oxidative decarboxylation of the peptide MftA. Abstract : Read the Commentary on this article at doi:10.1002/1873-3468.12281