The intrinsic stability of H2B-ubiquitylated nucleosomes and their in vitro assembly/disassembly by histone chaperone NAP1

• Published in: Biochimica et biophysica acta. General subjects Vol. 1864; no. 3; p. 129497
• Main Author: Krajewski, Wladyslaw A.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.03.2020
• Subjects: Chromatin; Hexasomes; histone code; Histones; mice; Nucleosomes; Ubiquitylation; Under “H2A/H2B stability/destabilization”; Chromatin; SDS; DTT; Ubiquitylation; PTM; Hexasomes; PAGE; Ub; bp; BSA; EMSA; Histones; Nucleosomes; EtBr

Apart the gene-regulatory functions as docking sites for histone ‘readers’, some histone modifications could directly affect nucleosome structure. The H2BK34-ubiquitylation deposited by MOF-MSL complex, increases nucleosome dynamics in vitro and promotes donation of one H2A/H2B dimer to histone acce...