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Chemical methods for studying the crosstalk between histone H2B ubiquitylation and H3 methylation.
Ai, Huasong; Peng, Shuai; Li, Jia-Bin.
Afiliação
  • Ai H; College of Pharmaceutical Sciences, Soochow University, Suzhou, China.
  • Peng S; Ministry of Education Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology, Department of Chemistry, Tsinghua University, Beijing, China.
  • Li JB; College of Pharmaceutical Sciences, Soochow University, Suzhou, China.
J Pept Sci ; 28(5): e3381, 2022 May.
Article em En | MEDLINE | ID: mdl-34811838
ABSTRACT
The reversible and dynamic post-translational modifications (PTMs) of histones in eukaryotic chromatin are intimately connected to cell development and gene function, and abnormal regulation of PTMs can result in cancer and neurodegenerative diseases. Specific combinations of these modifications are mediated by a series of chromatin proteins that write, erase, and read the "histone codes," but mechanistic studies of the precise biochemical and structural relationships between different sets of modifications and their effects on chromatin function constitute a unique challenge to canonical biochemical approaches. In the past decade, the development and application of chemical methods for investigating histone PTM crosstalks has received considerable attention in the field of chemical biology. In this review, taking the functional crosstalk between H2B ubiquitylation at Lys120 (H2BK120ub) and H3 methylation at Lys79 (H3K79me) as a typical example, we survey recent developments of different chemical methods, in particular, protein synthetic chemistry and protein-based chemical probes, for studying the mechanism of the functional crosstalks of histone PTMs.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Histonas / Processamento de Proteína Pós-Traducional Idioma: En Revista: J Pept Sci Assunto da revista: BIOQUIMICA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: China

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Histonas / Processamento de Proteína Pós-Traducional Idioma: En Revista: J Pept Sci Assunto da revista: BIOQUIMICA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: China