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Details

Autor(en) / Beteiligte
Titel
The YEATS Domain Histone Crotonylation Readers Control Virulence-Related Biology of a Major Human Pathogen
Ist Teil von
  • Cell reports (Cambridge), 2020-04, Vol.31 (3), p.107528-107528, Article 107528
Ort / Verlag
United States: Elsevier Inc
Erscheinungsjahr
2020
Quelle
MEDLINE
Beschreibungen/Notizen
  • Identification of multiple histone acylations diversifies transcriptional control by metabolism, but their functions are incompletely defined. Here we report evidence of histone crotonylation in the human fungal pathogen Candida albicans. We define the enzymes that regulate crotonylation and show its dynamic control by environmental signals: carbon sources, the short-chain fatty acids butyrate and crotonate, and cell wall stress. Crotonate regulates stress-responsive transcription and rescues C. albicans from cell wall stress, indicating broad impact on cell biology. The YEATS domain crotonylation readers Taf14 and Yaf9 are required for C. albicans virulence, and Taf14 controls gene expression, stress resistance, and invasive growth via its chromatin reader function. Blocking the Taf14 C terminus with a tag reduced virulence, suggesting that inhibiting Taf14 interactions with chromatin regulators impairs function. Our findings shed light on the regulation of histone crotonylation and the functions of the YEATS proteins in eukaryotic pathogen biology and fungal infections. [Display omitted] •Metabolism and stress responses control histone crotonylation in Candida albicans•The YEATS crotonylation readers Taf14 and Yaf9 are important for Candida virulence•Taf14 participates in stress responses, cell wall, and filamentation pathways•The SCFA crotonate affects transcription and stress susceptibility in Candida Diverse histone acylations expand functional linkages among metabolism, gene regulation, and cellular responses. Wang et al. report that metabolic and stress cues dynamically control histone crotonylation in the human commensal and pathogen Candida albicans and show the requirement for crotonylation readers in pathogenesis-related pathways and mammalian virulence.

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