Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 140, Issue 12, Pages 4200-4203Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b13506
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Funding
- National Institutes of Health (NIH) [F32 GM108275, F31 GM113486, R37 GM058822]
- NIH [S10 RR027109 A]
- NATIONAL CENTER FOR RESEARCH RESOURCES [S10RR027109] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM058822, F31GM113486, F32GM108275, R01GM058822] Funding Source: NIH RePORTER
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The dehydratase NisB performs stepwise tRNA(Glu)-dependent glutamylation of Ser/Thr residues and subsequent glutamate elimination to effect eight dehydrations in the biosynthesis of the antibacterial peptide nisin. Its substrate, NisA, bears a C-terminal core peptide that is modified and an N-terminal leader peptide (LP) that is not modified but that is required for efficient dehydration. To elucidate the mechanism of LP-NisB interactions during dehydration, we engineered a disulfide that covalently links the NisA LP to NisB. The enzyme fully dehydrated tethered NisA, confirming the functional LP binding site and supporting a mechanism where NisB uses a single LP binding site for glutamylation and elimination. We also show an order of NisA and tRNA(Glu) binding to NisB that enables dehydration.
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