Your browser doesn't support javascript.
loading
Histone PTM Crosstalk Stimulates Dot1 Methyltransferase Activity.
Cutler, Jevon A; Perner, Florian; Armstrong, Scott A.
Afiliación
  • Cutler JA; Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA.
  • Perner F; Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Internal Medicine C, Greifswald University Medical Center, Greifswald 17475, Germany.
  • Armstrong SA; Department of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Division of Hematology-Oncology, Boston Children's Hospital, Boston, MA 02115, USA. Electronic address: scott_armstrong@dfci.harvard.edu.
Trends Biochem Sci ; 46(7): 522-524, 2021 07.
Article en En | MEDLINE | ID: mdl-33879367
Valencia-Sánchez et al. have demonstrated that two histone post-translational modifications (PTMs) - H4K16 acetylation (H4K16ac) and H2BK120 ubiquitination (H2Bub) - enhance the methylation of H3K79 (H3K79me) by Dot1. This breakthrough indicates crosstalk between H4Kac/H2Bub/H3K79me and may improve our understanding of the role that Dot1/Dot1L plays in developmental processes and disease, including MLL1/KMT2A(MLL-r) leukemia.
Asunto(s)
Palabras clave
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Histonas / Procesamiento Proteico-Postraduccional Idioma: En Revista: Trends Biochem Sci Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Histonas / Procesamiento Proteico-Postraduccional Idioma: En Revista: Trends Biochem Sci Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos