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Histone H2A ubiquitination

The bulky nature of the ubiquitin adduct [403] and the site in histone H2A (K-119) where ubiquitination takes place (see Fig. 5) has fueled speculation that this [Pg.275]

Effect of the ionic strength (mM NaCl concentration) on the average sedimentation coelRcient (S20,w) of (208-12) oligonucleosome arrays reconstituted with HeLa cell native histone octamers [solid line, ], chicken erythrocyte histone octamers (broken line) [369], or hyperacetylated. HeLa cell histones 208-12 oligonucleosome complexes reconstituted with hyperacetylated HeLa cell histones ( ) [369]. [Pg.276]

Effect of the ionic strength on hyperacetylated 208-12 nucleosome arrays as visualized by electron microscopy. The numbers to the left indicate the milimolar NaCl concentration [369]. [Reproduced from Garcia-Ramirez M. et al. (1995) J. Biol. Chem. 270, 17923-17928, with permission from The American Society for Biochemistry and Molecular Biology.] [Pg.276]

In the early work on this topic, Kleinschmidt and Martinson [219] used reconstituted nucleosome core particles consisting of two uH2A molecules to find that these particles had structural features that were almost indistinguishable from those of particles reconstituted with native histones or from native nucleosome core particles. A more exhaustive and detailed study in the same topic carried out a few years later [220] came in corroboration of these results and showed that the same observations could be extended to nucleosomes reconstituted with uH2B. Furthermore, the NaCl dependent stability of the uH2A reconstituted nucleosome core particles is identical to that exhibited by the native counterpart [222]. [Pg.276]

In an attempt to study the role of this histone post-translational modification on the folding of the chromatin fiber, Jason et al. [221] performed a series of experiments using nucleosome arrays reconstituted onto the 208-12 DNA template. [Pg.276]


Analyses of the reeonstituted eomplexes by quantitative agarose gel electrophoresis [404,405] and analytical ultracentrifugation [266,406] in the presence of MgCl2 showed that the arrays were able to fold in a way that is almost indistinguishable from complexes reconstituted with major histones (see Fig. 14A-B). Despite this, it was found that histone H2A ubiquitination affects the MgCl2 solubility of the reconstituted complexes (see Fig. 14C) suggesting that this modification may play a role in enhancing the intermolecular associations between chromatin fibers [221]. [Pg.277]

Fig. 14. Effects of histone H2A ubiquitination on the folding and solubility of chromatin [221]. A. Magnesium chloride dependence of the sedimentation coefficient (S2o,w) of 208-12 nucleosome arrays. Sedimentation coefficients at a given magnesium chloride concentration are plotted relative... Fig. 14. Effects of histone H2A ubiquitination on the folding and solubility of chromatin [221]. A. Magnesium chloride dependence of the sedimentation coefficient (S2o,w) of 208-12 nucleosome arrays. Sedimentation coefficients at a given magnesium chloride concentration are plotted relative...

See other pages where Histone H2A ubiquitination is mentioned: [Pg.275]   
See also in sourсe #XX -- [ Pg.525 ]

See also in sourсe #XX -- [ Pg.525 ]

See also in sourсe #XX -- [ Pg.525 ]

See also in sourсe #XX -- [ Pg.525 ]




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