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Trends Biochem Sci. 2014 Nov;39(11):536-47. doi: 10.1016/j.tibs.2014.09.001. Epub 2014 Sep 29.

Structure and function of the nucleosome-binding PWWP domain.

Author information

1
Structural Genomics Consortium, University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada.
2
Structural Genomics Consortium, University of Toronto, 101 College Street, Toronto, Ontario M5G 1L7, Canada; Department of Physiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada. Electronic address: jr.min@utoronto.ca.

Abstract

PWWP domain-containing proteins are often involved in chromatin-associated biological processes, such as transcriptional regulation and DNA repair, and recent studies have shown that the PWWP domain specifies chromatin localization. Mutations in the PWWP domain, a 100-150 amino acid motif, have been linked to various human diseases, emphasizing its importance. Structural studies reveal that PWWP domains possess a conserved aromatic cage for histone methyl-lysine recognition, and synergistically bind both histone and DNA, which contributes to their nucleosome-binding ability and chromatin localization. Furthermore, the PWWP domain often cooperates with other histone and DNA 'reader' or 'modifier' domains to evoke crosstalk between various epigenetic marks. Here, we discuss these recent advances in understanding the structure and function of the PWWP domain.

KEYWORDS:

DNA binding; PWWP domain; crosstalk; epigenetic code; histone binding; nucleosome binding

PMID:
25277115
DOI:
10.1016/j.tibs.2014.09.001
[Indexed for MEDLINE]

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