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N-terminal acetylation of Set1-COMPASS fine-tunes H3K4 methylation patterns
- Title
- N-terminal acetylation of Set1-COMPASS fine-tunes H3K4 methylation patterns
- Authors
- Woo; Hyeonju; Oh; Junsoo; Cho; Yong-Joon; Goo Taeg; Kim; Seon-Young; Dan; Kisoon; Han; Dohyun; Lee; Jung-Shin; TaeSoo
- Ewha Authors
- 오구택; 김태수
- SCOPUS Author ID
- 오구택
; 김태수![scopus](/images/layout/icon2.png)
- Issue Date
- 2024
- Journal Title
- Science Advances
- ISSN
- 2375-2548
- Citation
- Science Advances vol. 10, no. 28
- Indexed
- SCIE; SCOPUS
![scopus](/images/layout/scopus2.gif)
- Document Type
- Article
- 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. © 2024 The Authors.
- DOI
- 10.1126/sciadv.adl6280
- Appears in Collections:
- 자연과학대학 > 생명과학전공 > Journal papers
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