期刊
NUCLEIC ACIDS RESEARCH
卷 50, 期 5, 页码 2549-2565出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkac077
关键词
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资金
- Science and Technology Planning Project of Shenzhen [JCYJ20180307155005435]
- Deutsche Forschungsgmeinschaft [SFB1064, SM426/1-1]
- FriedrichBauer-Stiftung [07/15]
- Wellcome Trust [203149, 104175/Z/14/Z]
- European Research Council [639253]
- Wellcome Trust through a Multi-User Equipment grant [101527/Z/13/Z]
- Deutsche Forschungsgemeinschaft
- Wellcome Trust [104175/Z/14/Z, 101527/Z/13/Z] Funding Source: Wellcome Trust
- European Research Council (ERC) [639253] Funding Source: European Research Council (ERC)
The Ioc4 subunit of the Isw1b chromatin-remodeling complex interacts with pre-existing histones and DNA through its PWWP domain, facilitating chromatin remodeling during transcription. The Ioc4-PWWP domain promotes efficient remodeling by Isw1b in vitro and maintains ordered chromatin structure in vivo.
The Isw1b chromatin-remodeling complex is specifically recruited to gene bodies to help retain pre-existing histones during transcription by RNA polymerase II. Recruitment is dependent on H3K36 methylation and the Isw1b subunit Ioc4, which contains an N-terminal PWWP domain. Here, we present the crystal structure of the Ioc4-PWWP domain, including a detailed functional characterization of the domain on its own as well as in the context of full-length Ioc4 and the Isw1b remodeler. The Ioc4-PWWP domain preferentially binds H3K36me3-containing nucleosomes. Its ability to bind DNA is required for nucleosome binding. It is also furthered by the unique insertion motif present in Ioc4-PWWP. The ability to bind H3K36me3 and DNA promotes the interaction of full-length Ioc4 with nucleosomes in vitro and they are necessary for its recruitment to gene bodies in vivo. Furthermore, a fully functional Ioc4-PWWP domain promotes efficient remodeling by Isw1b and the maintenance of ordered chromatin in vivo, thereby preventing the production of non-coding RNAs.
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