期刊
MOLECULAR CELL
卷 81, 期 17, 页码 3542-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2021.07.010
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资金
- Canadian Institutes of Health Research (CIHR) [MOP-162334]
- Natural Sciences and Engineering Research Council of Canada (NSERC) [RGPIN2018-04519]
- National Institutes of Health [GM132290-01]
- Calcul Quebec
- Compute Canada
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/S009035/1]
- Korean Foundation for Advanced Studies fellowship
- Alexander Graham Bell Canada Doctoral Scholarship from NSERC
- Fonds de Recherche Quebec -Sante (FRQS)
- BBSRC [BB/S009035/1] Funding Source: UKRI
Research has shown that the histone chaperone FACT binds to transcribed chromatin, predominantly recognizing the +1 nucleosome, as it is partially unwrapped by RNAPII, and spreads to downstream nucleosomes with the assistance of the chromatin remodeler Chd1.
The histone chaperone FACT occupies transcribed regions where it plays prominent roles in maintaining chromatin integrity and preserving epigenetic information. How it is targeted to transcribed regions, however, remains unclear. Proposed models include docking on the RNA polymerase II (RNAPII) C-terminal domain (CTD), recruitment by elongation factors, recognition of modified histone tails, and binding partially disassembled nucleosomes. Here, we systematically test these and other scenarios in Saccharomyces cerevisiae and find that FACT binds transcribed chromatin, not RNAPII. Through a combination of high-resolution genome-wide mapping, single-molecule tracking, and mathematical modeling, we propose that FACT recognizes the +1 nucleosome, as it is partially unwrapped by the engaging RNAPII, and spreads to downstream nucleosomes aided by the chromatin remodeler Chd1. Our work clarifies how FACT interacts with genes, suggests a processive mechanism for FACT function, and provides a framework to further dissect the molecular mechanisms of transcription-coupled histone chaperoning.
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