title: Studies on nuclease digestion of chromatin phosphorylated in vivo.
abstract: We have previously shown that, by culturing cells in hypertonic media, histone 2A becomes hyperphosphorylated (Pantazis, P., West, M. H. P., and Bonner, W. M. (1984) Mol. Cell. Biol. 4, 1186-1188). In the present study we have probed the effect of this histone modification on the overall chromatin structure by micrococcal nuclease and DNase I digestion. Although no significant quantitative differences in the extent of hydrolysis were observed between control and hyperphosphorylated chromatin by micrococcal nuclease, DNase I digested hyperphosphorylated chromatin at a 3- to 4-fold higher rate than unmodified chromatin.
authors.forename: M H
authors.initials: MH
authors.lastname: West
authors.forename: P
authors.initials: P
authors.lastname: Pantazis
authors.forename: W M
authors.initials: WM
authors.lastname: Bonner
mesh_terms: D000818:Animals; D002460:Cell Line; D002843:Chromatin / Q000378:metabolism*; D004247:DNA / Q000032:analysis; D003850:Deoxyribonuclease I / Q000378:metabolism*; D004492:Edetic Acid; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism; D007939:Leukemia L1210 / Q000378:metabolism; D051379:Mice; D008836:Micrococcal Nuclease / Q000378:metabolism*; D010472:Perchlorates; D010766:Phosphorylation
chemical_list: D002843:Chromatin; D006657:Histones; D010472:Perchlorates; D004247:DNA; D004492:Edetic Acid; D003850:Deoxyribonuclease I; D008836:Micrococcal Nuclease