Science and Technology Production
Article
Authorship
OCAMPO, JOSEFINA
;
Feng Cui
;
Victor B. Zurkin
;
Clark D J
Date
2016
Publishing House and Editing Place
Landes Bioscience
Magazine
nucleus,
vol. 7
(pp. 382-387)
- ISSN 1949-1034
Landes Bioscience
Landes Bioscience
ISSN
1949-1034
Summary
Information provided by the agent in
SIGEVA
Eukaryotic DNA is packaged into regularly spaced nucleosomes, resembling beads on a string. Each bead contains »147 bp wrapped around a core histone octamer. Linker histone (H1) binds to the linker DNA to drive chromatin folding. Micrococcal nuclease (MNase) digestion studies reveal 2 mono-nucleosomal intermediates: the core particle (»147 bp) and the chromatosome (»160 bp; a core particle with additional DNA protected by H1). We have recently developed an improved method for ...
Eukaryotic DNA is packaged into regularly spaced nucleosomes, resembling beads on a string. Each bead contains »147 bp wrapped around a core histone octamer. Linker histone (H1) binds to the linker DNA to drive chromatin folding. Micrococcal nuclease (MNase) digestion studies reveal 2 mono-nucleosomal intermediates: the core particle (»147 bp) and the chromatosome (»160 bp; a core particle with additional DNA protected by H1). We have recently developed an improved method for mapping nucleosomes, using exonuclease III to remove residual linker (MNase-Exo- seq).1 We discovered 2 new intermediate particles corresponding to core particles with »7 bp of linker protruding from one side (»154 bp) or both sides (»161 bp), which are formed in the absence of H1. We propose that these ?proto-chromatosomes? are stabilised by core histone-DNA contacts in the linker, »7 bp from the nucleosome boundaries. These contacts may determine the topography of the H1 binding site.
Show more
Show less
Key Words
LINKER HISTONENUCLEOSOMECHROMATOSOMENUCLEOSOME MAPINGCHROMATIN FOLDINGMNASE-SEQMNASE-EXO-SEQPROTO-CHROMATOSOME