Modulation of histone modifications and G-quadruplex structures by G-quadruplex-binding proteins

被引:10
作者
Oyoshi, Takanori [1 ]
Masuzawa, Tatsuki [1 ]
机构
[1] Shizuoka Univ, Grad Sch Sci, Dept Chem, 836 Ohya Suruga, Shizuoka 4228529, Japan
关键词
G-quadruplex binding protein; Epigenetics; RGG domain; RRM domain; INTRAMOLECULAR G-QUADRUPLEX; HUMAN TELOMERIC DNA; MYC G-QUADRUPLEX; RNA-BINDING; HNRNP A1; CRYSTAL-STRUCTURE; RGG DOMAIN; RECOGNITION; PROMOTER; IDENTIFICATION;
D O I
10.1016/j.bbrc.2020.02.178
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The functions of local conformations of non-B form DNA and RNA, such as the G-quadruplex, are thought to be regulated by their specific binding proteins. They regulate the formation of G-quadruplexes in cells and affect the biological functions of G-quadruplexes. Recent studies reported that G-quadruplexes regulate epigenetics through these G-quadruplex binding proteins. We discuss regulation of histone modifications through G-quadruplex RNA and its binding proteins which modulate the G-quadruplex conformations. G-quadruplex RNA is involved in telomere maintenance and transcription via histone modification. Furthermore, G-quadruplex binding proteins regulate formation and biological functions of G-quadruplexes through regulating their folding or unfolding. In this review, we will focus on the Gquadruplex binding proteins containing RRM and RGG domains. (C) 2020 Elsevier Inc. All rights reserved.
引用
收藏
页码:39 / 44
页数:6
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