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Histone acetylation and deacetylation - Mechanistic insights from structural biology.
Patel, Avinash B; He, Yuan; Radhakrishnan, Ishwar.
  • Patel AB; Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA. Electronic address: avinash.patel@northwestern.edu.
  • He Y; Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA. Electronic address: yuanhe@northwestern.edu.
  • Radhakrishnan I; Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA. Electronic address: i-radhakrishnan@northwestern.edu.
Gene ; 890: 147798, 2024 Jan 10.
Article en En | MEDLINE | ID: mdl-37726026
ABSTRACT
Histones are subject to a diverse array of post-translational modifications. Among them, lysine acetylation is not only the most pervasive and dynamic modification but also highly consequential for regulating gene transcription. Although enzymes responsible for the addition and removal of acetyl groups were discovered almost 30 years ago, high-resolution structures of the enzymes in the context of their native complexes are only now beginning to become available, thanks to revolutionary technologies in protein structure determination and prediction. Here, we will review our current understanding of the molecular mechanisms of acetylation and deacetylation engendered by chromatin-modifying complexes, compare and contrast shared features, and discuss some of the pressing questions for future studies.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Histonas / Procesamiento Proteico-Postraduccional Idioma: En Año: 2024 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Histonas / Procesamiento Proteico-Postraduccional Idioma: En Año: 2024 Tipo del documento: Article