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• W2031036160 abstract "FoxA1–3 (formerly HNF3α, -β, and -γ), members of the FoxA subfamily of forkhead transcription factors, function as initial chromatin-binding and chromatin-remodeling factors in a variety of tissues, including liver and pancreas. Despite essential roles in development and metabolism, regulation of FoxA factors is not well understood. This study examines a potential role for acetylation in the regulation of FoxA chromatin binding and remodeling. Using in silico analysis, we have identified 11 putative p300 acetylation sites within FoxA1, five of which are located within wings 1 and 2 of its winged-helix DNA-binding domain. These polypeptide structures stabilize FoxA DNA and chromatin binding, and we have demonstrated that acetylation attenuates FoxA binding to DNA and diminishes its ability to remodel chromatin. FoxA acetylation is inhibited by chromatin binding. We propose a model whereby stable chromatin binding protects the FoxA DNA-binding domain from acetylation to preserve chromatin binding and remodeling by FoxA factors in the absence of extracellular cues. FoxA1–3 (formerly HNF3α, -β, and -γ), members of the FoxA subfamily of forkhead transcription factors, function as initial chromatin-binding and chromatin-remodeling factors in a variety of tissues, including liver and pancreas. Despite essential roles in development and metabolism, regulation of FoxA factors is not well understood. This study examines a potential role for acetylation in the regulation of FoxA chromatin binding and remodeling. Using in silico analysis, we have identified 11 putative p300 acetylation sites within FoxA1, five of which are located within wings 1 and 2 of its winged-helix DNA-binding domain. These polypeptide structures stabilize FoxA DNA and chromatin binding, and we have demonstrated that acetylation attenuates FoxA binding to DNA and diminishes its ability to remodel chromatin. FoxA acetylation is inhibited by chromatin binding. We propose a model whereby stable chromatin binding protects the FoxA DNA-binding domain from acetylation to preserve chromatin binding and remodeling by FoxA factors in the absence of extracellular cues." @default.
• W2031036160 created "2016-06-24" @default.
• W2031036160 creator A5069952718 @default.
• W2031036160 creator A5072798746 @default.
• W2031036160 date "2010-01-01" @default.
• W2031036160 modified "2023-10-15" @default.
• W2031036160 title "Stable Chromatin Binding Prevents FoxA Acetylation, Preserving FoxA Chromatin Remodeling" @default.
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• W2031036160 doi "https://doi.org/10.1074/jbc.m109.063149" @default.
• W2031036160 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2804194" @default.
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• W2031036160 hasPublicationYear "2010" @default.
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