PWWP domains and their modes of sensing DNA and histone methylated lysines

Biophysics Reviews
Germana B RonaAnderson S Pinheiro

Abstract

Chromatin plays an important role in gene transcription control, cell cycle progression, recombination, DNA replication and repair. The fundamental unit of chromatin, the nucleosome, is formed by a DNA duplex wrapped around an octamer of histones. Histones are susceptible to various post-translational modifications, covalent alterations that change the chromatin status. Lysine methylation is one of the major post-translational modifications involved in the regulation of chromatin function. The PWWP domain is a member of the Royal superfamily that functions as a chromatin methylation reader by recognizing both DNA and histone methylated lysines. The PWWP domain three-dimensional structure is based on an N-terminal hydrophobic β-barrel responsible for histone methyl-lysine binding, and a C-terminal α-helical domain. In this review, we set out to discuss the most recent literature on PWWP domains, focusing on their structural features and the mechanisms by which they specifically recognize DNA and histone methylated lysines at the level of the nucleosome.

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Citations

Oct 16, 2018·Journal of Cellular Biochemistry·Germana B RonaAnderson S Pinheiro
Jun 20, 2020·Future Medicinal Chemistry·Brian M LinharesTomasz Cierpicki
Dec 11, 2019·Nature Structural & Molecular Biology·Haibo WangPatrick Cramer
Oct 18, 2018·Nature Communications·Stephanie LinkSandra B Hake
Nov 27, 2019·Nature Communications·Christian AlbigCatherine Regnard
May 17, 2017·Biophysics Reviews·Cris Dos Remedios
Mar 30, 2018·Frontiers in Chemistry·Wenchao LuCheng Luo
Dec 17, 2020·International Journal of Molecular Sciences·Marijn N MaasJasmin Mecinović
Dec 22, 2020·Frontiers in Physiology·Tamas Zakar, Jonathan W Paul
Apr 7, 2021·Current Opinion in Chemical Biology·Jinrong Min, Ke Liu

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