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Review
. 1978 Aug 16;20(3):159-66.
doi: 10.1007/BF00243762.

H2B nucleohistone-phospholipid interactions. Thermal denaturation and ultrastructural analysis

S Capitani, N M Maraldi, L Cocco, P Santi, F A Manzoli
Review

H2B nucleohistone-phospholipid interactions. Thermal denaturation and ultrastructural analysis

S Capitani et al. Mol Cell Biochem. .

Abstract

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.

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