Temperature-dependent cleavage of chromatin by micrococcal nuclease near the nucleosome center.
Digestion of nuclei at 4 degrees C with micrococcal nuclease results in significant intranucleosomal cleavage compared to digestion conducted at 37 degrees C. Employing nucleoprotein gel electrophoresis in one dimension followed by DNA electrophoresis in a second dimension, we demonstrate that such temperature-sensitive, internal cleavage predominantly occurs about 20 bp from the nucleosome center. We suggest that lower temperatures reduce the stability of hydrophobic interactions within the histone octamer and lead to a conformational alteration in nucleosomes that is detected by micrococcal nuclease.
D002478:Cells, Cultured; D002843:Chromatin / Q000378:metabolism*; D004247:DNA / Q000032:analysis; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008836:Micrococcal Nuclease / Q000378:metabolism*; D009707:Nucleosomes / Q000378:metabolism* / Q000648:ultrastructure; D010954:Plasmacytoma; D013696:Temperature
D002843:Chromatin; D009707:Nucleosomes; D004247:DNA; D008836:Micrococcal Nuclease