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

• Published in: Biochemical and biophysical research communications 2020-10, Vol.531 (1), p.39-44
• Main Authors: Oyoshi, Takanori, Masuzawa, Tatsuki
• Format: Article
• Language: English
• Subjects: Animals; Epigenesis, Genetic; Epigenetics; G-quadruplex binding protein; G-Quadruplexes; Histone Code; Humans; Protein Domains; Protein Unfolding; RGG domain; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - metabolism; RRM domain
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2020.02.178

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 G-quadruplex binding proteins containing RRM and RGG domains. •G-quadruplex RNA regulates histone modifications in conjunction with G-quadruplex RNA binding proteins.•The histone modifying enzyme with G-quadruplex RNA binding ability is recruited or removed by G-quadruplex RNA.•RNA recognition motif (RRM) and Arg-Gly-Gly (RGG) domain are conserved in both G-quadruplex folding and unfolding proteins.•G-quadruplex-specific binding abilities of TLS/FUS require RGG domain with a β-spiral structure.