Forkhead-associated proteins genetically linked to the serine/threonine kinase PknB regulate carbon flux towards antibiotic biosynthesis in Streptomyces coelicolor.
Bottom Line: Here we report functional analysis of pknB and two linked genes, fhaAB, encoding forkhead-associated (FHA) domain proteins that are part of a highly conserved gene locus in actinobacteria.FhaAB are candidate interacting partners of PknB and loss of their function resulted in deregulation of central carbon metabolism, with carbon flux diverted to synthesis of the antibiotic actinorhodin.The results indicate that inactivation of FHA 'brake' proteins can potentially amplify the function of STPKs and, in this case, provide a means to overproduce antibiotics.
Affiliation: Institute of Life Science, Swansea University, Singleton Park, Swansea SA28PP, UK.Show MeSH
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Mentions: PknB is predicted to be a 673‐amino‐acid membrane protein with the ability to autophosphorylate. To investigate these properties, recombinant N‐terminal His‐tagged PknB was expressed in E. coli BL21. After fractionation and Western blotting with an antibody to detect the His‐tagged protein, PknB was predominantly found to be enriched in membrane fractions from E. coli (Fig. 3), migrating with an apparent approximate molecular mass of 130 kDa.
Affiliation: Institute of Life Science, Swansea University, Singleton Park, Swansea SA28PP, UK.