Studies on nuclease digestion of chromatin phosphorylated in vivo.
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.
West
M H
MH
Pantazis
P
P
Bonner
W M
WM
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
D002843:Chromatin; D006657:Histones; D010472:Perchlorates; D004247:DNA; D004492:Edetic Acid; D003850:Deoxyribonuclease I; D008836:Micrococcal Nuclease