JadX is a disparate natural product binding protein

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DOIResolve DOI: http://doi.org/10.1021/jacs.5b11286
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TypeArticle
Journal titleJournal of the American Chemical Society
ISSN0002-7863
1520-5126
Volume138
Issue7
Pages22002208
AbstractWe report that JadX, a protein of previously undetermined function coded for in the jadomycin biosynthetic gene cluster of Streptomyces venezuelae ISP5230, affects both chloramphenicol and jadomycin production levels in blocked mutants. Characterization of recombinant JadX through protein–ligand interactions by chemical shift perturbation and WaterLOGSY NMR spectroscopy resulted in the observation of binding between JadX and a series of jadomycins and between JadX and chloramphenicol, another natural product produced by S. venezuelae ISP5230. These results suggest JadX to be an unusual class of natural product binding protein involved in binding structurally disparate natural products. The ability for JadX to bind two different natural products in vitro and the ability to affect production of these secondary metabolites in vivo suggest a potential role in regulation or signaling. This is the first example of functional characterization of these JadX-like proteins, and provides insight into a previously unobserved regulatory process.
Publication date
PublisherACS Publications
LanguageEnglish
AffiliationNational Research Council Canada; Aquatic and Crop Resource Development
Peer reviewedYes
NPARC number23000138
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Record identifier1cef32c4-4c83-4b35-af83-2602ff6d1af3
Record created2016-06-07
Record modified2016-06-07
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