Literature DB >> 25277115

Structure and function of the nucleosome-binding PWWP domain.

Su Qin1, Jinrong Min2.   

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.
Copyright © 2014 Elsevier Ltd. All rights reserved.

Entities:  

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

Mesh:

Substances:

Year:  2014        PMID: 25277115     DOI: 10.1016/j.tibs.2014.09.001

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  62 in total

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3.  Buried in PEAT-discovery of a new silencing complex with opposing activities.

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4.  Drosophila P75 safeguards oogenesis by preventing H3K9me2 spreading.

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5.  A PWWP Domain of Histone-Lysine N-Methyltransferase NSD2 Binds to Dimethylated Lys-36 of Histone H3 and Regulates NSD2 Function at Chromatin.

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Authors:  Leilei Shi; Hong Wen; Xiaobing Shi
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Review 9.  PWWP domains and their modes of sensing DNA and histone methylated lysines.

Authors:  Germana B Rona; Elis C A Eleutherio; Anderson S Pinheiro
Journal:  Biophys Rev       Date:  2016-01-14

10.  ZCWPW1 is recruited to recombination hotspots by PRDM9 and is essential for meiotic double strand break repair.

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