The macromolecular complexes of histones affect protein arginine methyltransferase activities.

Fulton, Melody D; Cao, Mengtong; Ho, Meng-Chiao; Zhao, Xinyang; Zheng, Y George

Fulton, Melody D; Cao, Mengtong; Ho, Meng-Chiao; Zhao, Xinyang; Zheng, Y George.

Afiliación

Fulton MD; Department of Pharmaceutical and Biomedical Sciences, College of Pharmacy, The University of Georgia, Athens, Georgia, USA.
Cao M; Department of Pharmaceutical and Biomedical Sciences, College of Pharmacy, The University of Georgia, Athens, Georgia, USA.
Ho MC; Institute of Biological Chemistry, Academia Sinica, Nankang, Taipei, Taiwan.
Zhao X; Department of Biochemistry and Molecular Genetics, The University of Alabama at Birmingham, Birmingham, Alabama, USA.
Zheng YG; Department of Pharmaceutical and Biomedical Sciences, College of Pharmacy, The University of Georgia, Athens, Georgia, USA. Electronic address: yzheng@uga.edu.

J Biol Chem ; 297(4): 101123, 2021 10.

Article en En | MEDLINE | ID: mdl-34492270

Asunto(s)

Histonas/química; Complejos Multiproteicos/química; Proteína-Arginina N-Metiltransferasas/química; Arginina/química; Arginina/genética; Arginina/metabolismo; Histonas/genética; Histonas/metabolismo; Humanos; Complejos Multiproteicos/genética; Complejos Multiproteicos/metabolismo; Estructura Cuaternaria de Proteína; Proteína-Arginina N-Metiltransferasas/genética; Proteína-Arginina N-Metiltransferasas/metabolismo; Especificidad por Sustrato

Palabras clave

PRMT; arginine methylation; epigenetics; histone; nucleosome; octamer

Texto completo

Imprimir

XML

PubMed Links

Buscar en Google

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteína-Arginina N-Metiltransferasas / Histonas / Complejos Multiproteicos Límite: Humans Idioma: En Revista: J Biol Chem Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo

Imprimir

XML

PubMed Links

Buscar en Google