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H2B nucleohistone — phospholipid interactions. Thermal denaturation and ultrastructural analysis

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Summary

Sphingomyelin, phosphatidylserine, bovine lecithin and phosphatidylethanolamine modify the thermal stability of H2B-DNA complexes, by inducing stabilization at 0.3 and 0.6 H2B:DNA weight ratios and destabilization at 0.8, 1.0 and 1.5 ones.

The ability of phospholipids to modify 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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Author notes

  1. F. A. Manzoli

    Present address: Istituti di Anatomia, Umana Normale, Facolta di Medicina, Via Itnerio, 48 40126, Bologna, Italy

Authors and Affiliations

  1. Istituti di Istologia ed Embriologia generale, Facoltà di Medicina, Università di Chieti, Ancona

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

  2. Istituti di Anatomia Umana Normale, Facoltà di Medicina, Università di Bologna, Chieti, Italy

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

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  5. F. A. Manzoli
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Capitani, S., Maraldi, N.M., Cocco, L. et al. H2B nucleohistone — phospholipid interactions. Thermal denaturation and ultrastructural analysis. Mol Cell Biochem 20, 159–166 (1978). https://doi.org/10.1007/BF00243762

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  • DOI: https://doi.org/10.1007/BF00243762

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