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• W2013036895 abstract "Cobalamin (B 12 ) typically functions as an enzyme cofactor but can also regulate gene expression via RNA-based riboswitches. B 12 -directed gene regulatory mechanisms via protein factors have, however, remained elusive. Recently, we reported down-regulation of a light-inducible promoter in the bacterium Myxococcus xanthus by two paralogous transcriptional repressors, of which one, CarH, but not the other, CarA, absolutely requires B 12 for activity even though both have a canonical B 12 -binding motif. Unanswered were what underlies this striking difference, what is the specific cobalamin used, and how it acts. Here, we show that coenzyme B 12 (5′-deoxyadenosylcobalamin, AdoB 12 ), specifically dictates CarH function in the dark and on exposure to light. In the dark, AdoB 12 -binding to the autonomous domain containing the B 12 -binding motif foments repressor oligomerization, enhances operator binding, and blocks transcription. Light, at various wavelengths at which AdoB 12 absorbs, dismantles active repressor oligomers by photolysing the bound AdoB 12 and weakens repressor–operator binding to allow transcription. By contrast, AdoB 12 alters neither CarA oligomerization nor operator binding, thus accounting for its B 12 -independent activity. Our findings unveil a functional facet of AdoB 12 whereby it serves as the chromophore of a unique photoreceptor protein class acting in light-dependent gene regulation. The prevalence of similar proteins of unknown function in microbial genomes suggests that this distinct B 12 -based molecular mechanism for photoregulation may be widespread in bacteria." @default.
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• W2013036895 date "2011-04-18" @default.
• W2013036895 modified "2023-10-17" @default.
• W2013036895 title "Light-dependent gene regulation by a coenzyme B ₁₂ -based photoreceptor" @default.
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• W2013036895 doi "https://doi.org/10.1073/pnas.1018972108" @default.
• W2013036895 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3088613" @default.
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