H2B nucleohistone-phospholipid interactions. Thermal denaturation and ultrastructural analysis.
Sphingomyelin, phosphatidylserine, bovine lecithin and phosphatidylethanolamine modify the thermal stabilization of H2B-DNA complexes, by inducing stabilization at 0.3 and 0.6 H2B : DNA weight ratios and destabilify the arrangement of nucleohistone is confirmed by ultrastructural analysis which indicates a competitive action of these molecules during the nucleoprotein assembly. A possible regulatory role of phospholipids on native chromatin is proposed.
D002843:Chromatin / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D004247:DNA / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D006358:Hot Temperature; D008854:Microscopy, Electron; D009691:Nucleic Acid Denaturation / Q000187:drug effects; D010743:Phospholipids / Q000378:metabolism* / Q000494:pharmacology; D011489:Protein Denaturation / Q000187:drug effects
D002843:Chromatin; D006657:Histones; D010743:Phospholipids; D004247:DNA