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Nucleic Acids Res., Dec 16 2024, gkae1229 | https://doi.org/10.1093/nar/gkae1229
Abo1 ATPase facilitates the dissociation of FACT from chromatin
Juwon Jang 1,†, Yujin Kang2,†, Martin Zofall3, Sangmin Woo1, Soyeong An2, Carol Cho1, Shiv Grewal 3, Ja Yil Lee 2,* and Ji-Joon Song 1,*
1Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), KI for the BioCentury, 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Korea
2Department of Biological Sciences, Ulsan National Institute of Science and Technology, 50, UNIST-gil, Eonyang-eup, Ulju-gun, Ulsan, 44919, Korea
3Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA
*To whom correspondence should be addressed. : Ji-Joon Song
Correspondence may also be addressed to Ja Yil Lee.
†The first two authors should be regarded as Joint First Authors.
1Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), KI for the BioCentury, 291 Daehak-ro, Yuseong-gu, Daejeon 34141, Korea
2Department of Biological Sciences, Ulsan National Institute of Science and Technology, 50, UNIST-gil, Eonyang-eup, Ulju-gun, Ulsan, 44919, Korea
3Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA
*To whom correspondence should be addressed. : Ji-Joon Song
Correspondence may also be addressed to Ja Yil Lee.
†The first two authors should be regarded as Joint First Authors.
Abstract
The histone chaperone FAcilitates Chromatin Transcription (FACT) is a heterodimeric complex consisting of Spt16 and Pob3, crucial for preserving nucleosome integrity during transcription and DNA replication. Loss of FACT leads to cryptic transcription and heterochromatin defects. FACT was shown to interact with Abo1, an AAA + family histone chaperone involved in nucleosome dynamics. Depletion of Abo1 causes FACT to stall at transcription start sites and mimics FACT mutants, indicating a functional association between Abo1 and FACT. However, the precise role of Abo1 in FACT function remains poorly understood. Here, we reveal that Abo1 directly interacts with FACT and facilitates the dissociation of FACT from nucleosome. Specifically, the N-terminal region of Abo1 utilizes its FACT-interacting helix to bind to the N-terminal domain of Spt16. In addition, using single-molecule fluorescence imaging, we discovered that Abo1 facilitates the ATP-dependent dissociation of FACT from nucleosomes. Furthermore, we demonstrate that the interaction between Abo1 and FACT is essential for maintaining heterochromatin in fission yeast. In summary, our findings suggest that Abo1 regulates FACT turnover in an ATP-dependent manner, proposing a model of histone chaperone recycling driven by inter-chaperone interactions.
논문정보
- Research article
- 2024년 12월 (BRIC 등록일 2024-12-18)
- 국내(교신)+국외 연구진
- 생명과학 > 구조생물 및 생물물리학
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