期刊
CURRENT OPINION IN CHEMICAL BIOLOGY
卷 63, 期 -, 页码 105-114出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2021.02.018
关键词
Chromatin; Nucleosome; Histone; Complex structure
资金
- AbbVie
- Bayer Pharma AG
- Boehringer Ingelheim
- Canada Foundation for Innovation
- Eshelman Institute for Innovation
- Genome Canada through Ontario Genomics Institute [OGI-055]
- Innovative Medicines Initiative (EU/EFPIA) (ULTRA-DD grant) [115766]
- Janssen
- Merck KGaA, Darmstadt, Germany
- MSD
- Novartis Pharma AG
- Ontario Ministry of Research, Innovation and Science (MRIS)
- Pfizer
- Sao Paulo Research Foundation-FAPESP
- Takeda
- Wellcome
- National Natural Science Foundation of China [31770834]
The dynamic regulation of chromatin structure by various modulators is crucial for downstream DNA processes, and understanding the 3D structures of these modulators in complex with nucleosome is essential for studying chromatin structure changes. Recent progress has been made in structural studies of selected chromatin modulators interacting with nucleosome.
The chromatin structure is dynamically regulated by many different modulators that post-translationally modify histones, replace canonical histones with histone variants, and unwind nucleosomal DNA, thereby modulating the accessibility of nucleosomal DNA and facilitating downstream DNA-templated nuclear processes. To understand how these modulators change the chromatin structure, it is essential to determine the 3D structures of chromatin modulators in complex with nucleosome. Here, we review the very recent progress in structural studies of some selected chromatin modulators in complex with nucleosome, including those of histone demethylases LSD1/2, some pioneer transcription factors, and the PWWP domain-containing protein LEDGF.
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