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Partial characterization of nuclear binding sites for retinol delivered by cellular retinol binding protein.

Abstract：

:Retinol (vitamin A alcohol), which plays an important role in the differentiation of epithelia, can be transferred to chromatin in vitro. Rat liver chromatin can accept retinol in a specific and saturable manner only when the retinol is presented as a complex with cellular retinol-binding protein (CRBP). A partial characterization of the nuclear components responsible for accepting retinol is reported here. A preparation of solubilized chromatin isolated from liver nuclei was able to accept retinol from its complex with CRBP as described previously for nuclei and chromatin. The binding of retinol to chromatin was noncovalent. However, chromatin prepared from nuclei which were incubated with DNase I or micrococcal nuclease did not accept retinol specifically. Chromatin in the form of mono and dinucleosomes also did not accept retinol. However, treatment of nuclei with RNase did not affect the specific binding of retinol. Furthermore, it has been found that retinol was not transferred to purified double or single stranded DNA. These results are interpreted to indicate that the transfer of retinol to specific nuclear binding sites requires a higher order of chromatin structure than that occurring in nucleosome preparations.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Liau G,Ong DE,Chytil F

doi

10.1016/0003-9861(85)90287-5

subject

Has Abstract

pub_date

1985-03-01 00:00:00

pages

354-60

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(85)90287-5

journal_volume

237

pub_type

杂志文章

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