JadX is a Disparate Natural Product Binding Protein
| Autor: | Raymond T. Syvitski, Camilo F. Martinez-Farina, Stephanie M. Forget, Andrew W. Robertson, Nicole E. McCormick, David L. Jakeman |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Streptomyces venezuelae Mutant Molecular Conformation Biochemistry Catalysis law.invention 03 medical and health sciences chemistry.chemical_compound Colloid and Surface Chemistry law Gene cluster medicine Nuclear Magnetic Resonance Biomolecular Biological Products Natural product biology Binding protein Chloramphenicol General Chemistry Isoquinolines biology.organism_classification Recombinant Proteins Streptomyces In vitro 030104 developmental biology chemistry Recombinant DNA Carrier Proteins medicine.drug |
| Zdroj: | Journal of the American Chemical Society. 138:2200-2208 |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/jacs.5b11286 |
| Popis: | We 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. |
| Databáze: | OpenAIRE |
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