Your browser doesn't support javascript.
loading
Total chemical synthesis of sumoylated histone H4 reveals negative biochemical crosstalk with histone ubiquitylation.
Singh, Sumeet K; Reyna, Andres; Xie, Xiaowen; Mao, Haibin; Ji, Meihuan; Zheng, Ning; Hsu, Peter L; Chatterjee, Champak.
Afiliação
  • Singh SK; Department of Chemistry, University of Washington, Seattle 98195, USA. champak1@uw.edu.
  • Reyna A; Department of Chemistry, University of Washington, Seattle 98195, USA. champak1@uw.edu.
  • Xie X; Department of Pharmacology, University of Washington; Howard Hughes Medical Institute, University of Washington, Seattle 98195, USA.
  • Mao H; Department of Pharmacology, University of Washington; Howard Hughes Medical Institute, University of Washington, Seattle 98195, USA.
  • Ji M; Department of Chemistry, University of Washington, Seattle 98195, USA. champak1@uw.edu.
  • Zheng N; Department of Pharmacology, University of Washington; Howard Hughes Medical Institute, University of Washington, Seattle 98195, USA.
  • Hsu PL; Department of Pharmacology, University of Washington; Howard Hughes Medical Institute, University of Washington, Seattle 98195, USA.
  • Chatterjee C; Department of Chemistry, University of Washington, Seattle 98195, USA. champak1@uw.edu.
Chem Commun (Camb) ; 59(27): 4063-4066, 2023 Mar 30.
Article em En | MEDLINE | ID: mdl-36938583
An efficient total chemical synthesis of site-specifically sumoylated histone H4 was undertaken to generate homogenously modified mononucleosomes. These were tested as substrates in biochemical assays with the histone H2B-specific ubiquitin ligases Rad6 and Bre1, which revealed the strong inhibition of H2B ubiquitylation by SUMO. This novel negative biochemical crosstalk between SUMO and ubiquitin was also confirmed to exist in human cells.
Assuntos
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Histonas / Proteínas de Saccharomyces cerevisiae Limite: Humans Idioma: En Revista: Chem Commun (Camb) Assunto da revista: QUIMICA Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos País de publicação: Reino Unido
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Histonas / Proteínas de Saccharomyces cerevisiae Limite: Humans Idioma: En Revista: Chem Commun (Camb) Assunto da revista: QUIMICA Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos País de publicação: Reino Unido