[Cangen-L) Histones article and supporting documents
- From: Rievaulx Canines <rievaulx@xxxxxxxxxxxxx>
- To: cangen-L@xxxxxxxxxxxxx
- Date: Sat, 20 Jul 2002 07:42:07 -0700
Fig. 6. Characterization of recombinant histone octamers. SDS/PAGE (15%
gel) and Coomassie blue staining of histone octamers assembled from
bacterially
expressed wild-type (WT) Drosophila histones or histones lacking
N-terminal tails, as indicated. G, globular domain.
Fig. 7. Nucleosome sliding is not affected by acetylation of histones by
p300. (A) hsp70 nucleosomes (359 bp) assembled from nonacetylated
recombinant histones
(nAC) and nucleosomes containing histones hyperacetylated by p300 (AC)
were analyzed by native two-dimensional (2D) gel electrophoresis. (B)
Extent of histone
acetylation. Histones acetylated by p300 were analyzed by denaturing 2D
gel electrophoresis (first-dimension SDS; second-dimension Acetic
acid--urea--cetyltrimethylammonium bromide) and Coomassie blue staining.
The electrophoretic positions of nonacetylated and multiply acetylated
core histones are
indicated (1).
Reference:
1. Rogakou, E. P., Redon, C., Boon, C., Johnson, K. & Bonner, W. M.
(2000) BioTechniques 28, 38-40, 42, 46.
Fig. 8. Requirement of histone H4 16-KRHR-19 for the stimulation of the
ATPase activity of NURF. Mononucleosomes reconstituted from wild-type or
mutant
histones were assayed for the ability to stimulate NURF ATPase activity.
Hydrolysis of [a-32P]ATP to [a-32P]ADP is measured by TLC. Conditions of
assay are
as in Fig. 4.
Other related posts:
- » [Cangen-L) Histones article and supporting documents
