Mycofactocin Biosynthesis: Modification of the Peptide MftA by the Radical S-adenosylmethionine Protein MftC

Authors

Bulat Khaliullin, University of Denver
Priyanka Aggarwal, University of Denver
Michael Bubas, University of Denver
Gareth R. Eaton, University of DenverFollow
Sandra S. Eaton, University of DenverFollow
John A. LathamFollow

Publication Date

8-2016

Document Type

Article

Organizational Units

College of Natual Science and Mathematics, Chemistry and Biochemistry

Keywords

Mycofactocin, Peptide interaction, Radical S‐adenosylmethionine

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 KD (~ 100 nm) and MftC with a low micromolar KD (~ 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.

Publication Statement

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Recommended Citation

Khaliullin, B., Aggarwal, P., Bubas, M., Eaton, G. R., Eaton, S. S., & Latham, J. A. (2016). Mycofactocin biosynthesis: Modification of the peptide MftA by the radical S-adenosylmethionine protein MftC. FEBS Letters, 590(16), 2538-2548. DOI: 10.1002/1873-3468.12249.