Journal
BIOCHEMISTRY
Volume 48, Issue 27, Pages 6502-6507Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi9004304
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Funding
- National Science Fond, Ministry of Education, Bulgaria [TKB 1608]
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The participation of HMGB-1 and -2 proteins in chromatin remodeling is investigated. Here, the ability of these proteins and their posttranslationally acetylated forms to affect SWI/SNF and RSC-dependent nucleosome mobilization was studied. Both proteins assisted nucleosome sliding induced by the two remodelers. Following acetylation, these proteins acquire the ability to bind to core particles, a property that has not yet been documented with parental proteins. We further report that compared to the nonmodified proteins, acetylated HMGB-1 and -2 exhibited both stronger binding to linker DNA-containing nucleosomes and a higher co-remodeling activity. Acetylation of HMGB-I and -2 proteins enhanced binding of SWI/SNF to the nucleosome but did not affect its ATPase activity.
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