Regulation of acetohydroxy acid synthase activities in adenyl cyclase-deficient strains of Escherichia coli K-12.
Previous findings suggested that cyclic AMP was involved in the regulation of ilvB(AHASI) only and that ilvG (AHASII) and ilvHI (AHASIII) were not controlled by this nucleotide. In this study, derepression patterns of total AHAS activities (ilvB and ilvHI) in adenyl cyclase-negative strains (i.e. cya-) were substantially reduced as contrasted with AHAS activity observed for cya+ strains. Further, the parental strains (cya+) consistently exhibited higher levels of AHAS activity than mutant strains (cya-) during carbon and energy downshifts. Other data suggested that the valine derepression signal could not override the necessity for cya gene product to yield maximal derepression of AHAS gene activities. Cyclic AMP stimulated AHAS gene activities under both in vivo and in vitro assay conditions. Thus, these data provide evidence for an absolute requirement of cAMP for maximal expression of the genes encoding for AHAS activities of E. coli K-12.
D000095:Acetolactate Synthase / Q000096:biosynthesis*; D000262:Adenylyl Cyclases / Q000172:deficiency; D000242:Cyclic AMP / Q000502:physiology*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005786:Gene Expression Regulation / Q000187:drug effects; D006159:Guanosine Tetraphosphate / Q000494:pharmacology; D007532:Isoleucine / Q000235:genetics*; D009876:Operon; D007652:Oxo-Acid-Lyases / Q000096:biosynthesis*; D014633:Valine / Q000235:genetics*
D007532:Isoleucine; D006159:Guanosine Tetraphosphate; D000242:Cyclic AMP; D000095:Acetolactate Synthase; D007652:Oxo-Acid-Lyases; D000262:Adenylyl Cyclases; D014633:Valine