Transcription-facilitating histone chaperons interact with genomic and synthetic G4 structures

Affinity for G-quadruplex (G4) structures may be a common feature of transcription-facilitating histone chaperons (HCs). This assumption is based on previous unmatched studies of HCs FACT, nucleolin (NCL), BRD3, and ATRX. We verified this assumption and considered its implications for the therapeuti...

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Veröffentlicht in:	International journal of biological macromolecules 2020-10, Vol.160, p.1144-1157
Hauptverfasser:	Pavlova, Iulia I., Tsvetkov, Vladimir B., Isaakova, Ekaterina A., Severov, Vyacheslav V., Khomyakova, Ekaterina A., Lacis, Ivan A., Lazarev, Vassilii N., Lagarkova, Maria A., Pozmogova, Galina E., Varizhuk, Anna M.
Format:	Artikel
Sprache:	eng
Schlagworte:	A549 Cells Binding Sites C-Myc Cells, Cultured DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism G-Quadruplexes Genes, myc Hep G2 Cells High Mobility Group Proteins - chemistry High Mobility Group Proteins - metabolism Histone Chaperones - chemistry Histone Chaperones - metabolism Histone chaperons HT29 Cells Humans Molecular Docking Simulation Nucleolin Phosphoproteins - chemistry Phosphoproteins - metabolism Protein Binding RNA-Binding Proteins - chemistry RNA-Binding Proteins - metabolism Transcription Factors - chemistry Transcription Factors - metabolism Transcriptional Elongation Factors - chemistry Transcriptional Elongation Factors - metabolism X-linked Nuclear Protein - chemistry X-linked Nuclear Protein - metabolism
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