4.5 Review

Structures of chromatin modulators in complex with nucleosome

Journal

CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 63, Issue -, Pages 105-114

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2021.02.018

Keywords

Chromatin; Nucleosome; Histone; Complex structure

Funding

  1. AbbVie
  2. Bayer Pharma AG
  3. Boehringer Ingelheim
  4. Canada Foundation for Innovation
  5. Eshelman Institute for Innovation
  6. Genome Canada through Ontario Genomics Institute [OGI-055]
  7. Innovative Medicines Initiative (EU/EFPIA) (ULTRA-DD grant) [115766]
  8. Janssen
  9. Merck KGaA, Darmstadt, Germany
  10. MSD
  11. Novartis Pharma AG
  12. Ontario Ministry of Research, Innovation and Science (MRIS)
  13. Pfizer
  14. Sao Paulo Research Foundation-FAPESP
  15. Takeda
  16. Wellcome
  17. National Natural Science Foundation of China [31770834]

Ask authors/readers for more resources

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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