In vivo binding of retinol to chromatin. The binding is mediated by a lipoprotein

N. Ferrari, U. Pfeffer, G. Vidali

Research output: Contribution to journalArticlepeer-review


We have previously shown that exposure of responding cells to vitamin A leads to profound modifications of chromatin structure as revealed by an increased susceptiblity to DNase I digestion, modified patterns of histone acetylation, and impaired synthesis of a nonhistone chromosomal protein (Ferrari, N., and Vidali, g. (1985) Eur. J. Biochem. 151, 305-310). The present results show that these effects are most probably due to the direct interaction between retinol and chromatin, and analysis of mononucleosomes and higher oligomers obtained from retinol-treated cells shows that retinol is indeed tightly bound to chromatin. Enzymatic digestions of vitamin A containing nucleosomes with proteinase K, phospholipase C, and phospholipase A2 support a model where the final binding of retinol to chromatin is mediated by a lipoprotein: the recognition of the binding sites on DNA being dictated by the proteic component while the hydrophobic retinol is solubilized in the fatty acid moiety.

Original languageEnglish
Pages (from-to)448-453
Number of pages6
JournalJournal of Biological Chemistry
Issue number1
Publication statusPublished - 1988

ASJC Scopus subject areas

  • Biochemistry


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