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N-terminal acetylation of Set1-COMPASS fine-tunes H3K4 methylation patterns.
Woo, Hyeonju; Oh, Junsoo; Cho, Yong-Joon; Oh, Goo Taeg; Kim, Seon-Young; Dan, Kisoon; Han, Dohyun; Lee, Jung-Shin; Kim, TaeSoo.
Afiliación
  • Woo H; Department of Life Science and Multitasking Macrophage Research Center, Ewha Womans University, Seoul 03760, Republic of Korea.
  • Oh J; Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University, Chuncheon 24341, Republic of Korea.
  • Cho YJ; Department of Molecular Bioscience, College of Biomedical Science, Kangwon National University, Chuncheon 24341, Republic of Korea.
  • Oh GT; Multidimensional Genomics Research Center, Kangwon National University, Chuncheon, Republic of Korea.
  • Kim SY; Department of Life Science and Multitasking Macrophage Research Center, Ewha Womans University, Seoul 03760, Republic of Korea.
  • Dan K; Korea Bioinformation Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Republic of Korea.
  • Han D; Proteomics Core Facility, Biomedical Research Institute, Seoul National University Hospital, Seoul 03082, Republic of Korea.
  • Lee JS; Proteomics Core Facility, Biomedical Research Institute, Seoul National University Hospital, Seoul 03082, Republic of Korea.
  • Kim T; Department of Transdisciplinary Medicine, Seoul National University Hospital, Seoul 03082, Republic of Korea.
Sci Adv ; 10(28): eadl6280, 2024 Jul 12.
Article en En | MEDLINE | ID: mdl-38996018
ABSTRACT
H3K4 methylation by Set1-COMPASS (complex of proteins associated with Set1) is a conserved histone modification. Although it is critical for gene regulation, the posttranslational modifications of this complex that affect its function are largely unexplored. This study showed that N-terminal acetylation of Set1-COMPASS proteins by N-terminal acetyltransferases (NATs) can modulate H3K4 methylation patterns. Specifically, deleting NatA substantially decreased global H3K4me3 levels and caused the H3K4me2 peak in the 5' transcribed regions to shift to the promoters. NatA was required for N-terminal acetylation of three subunits of Set1-COMPASS Shg1, Spp1, and Swd2. Moreover, deleting Shg1 or blocking its N-terminal acetylation via proline mutation of the target residue drastically reduced H3K4 methylation. Thus, NatA-mediated N-terminal acetylation of Shg1 shapes H3K4 methylation patterns. NatB also regulates H3K4 methylation, likely via N-terminal acetylation of the Set1-COMPASS protein Swd1. Thus, N-terminal acetylation of Set1-COMPASS proteins can directly fine-tune the functions of this complex, thereby substantially shaping H3K4 methylation patterns.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Histonas / N-Metiltransferasa de Histona-Lisina / Proteínas de Saccharomyces cerevisiae Idioma: En Revista: Sci Adv Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Histonas / N-Metiltransferasa de Histona-Lisina / Proteínas de Saccharomyces cerevisiae Idioma: En Revista: Sci Adv Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos