Title

Bipartite structure of the proximal promoter of a human H4 histone gene

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Cell Biology

Publication Date

1995-07-01

Document Type

Article

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The proximal promoter of the human H4 histone gene FO108 contains two regions of in vivo protein-DNA interaction, Sites I and II. Electrophoretic mobility shift assays using a radiolabeled DNA probe revealed that several proteins present in HeLa cell nuclear extracts bound specifically to Site I (nt-125 to nt-86). The most prominent complex, designated HiNF-C, and a complex of greater mobility, HiNF-C', were specifically compatable by an Sp1 consensus oligonucleotide. Fractionation of HiNF-C using wheat germ agglutinin affinity chromatography suggested that, like Sp1, HiNF-C contains N-acetylglucosamine moieties. Two minor complexes of even greater mobility, designated HiNF-E and F, were compatable by ATF consensus oligonucleotides. A DNA probe carrying a site-specific mutation in the distal portion of Site I failed to bind HiNF-E, indicating that this protein associated specifically to this region. UV cross-linking analysis showed that several proteins of different molecular weights interact specifically with Site I. These data indicate that Site I possesses a bipartite structure and that multiple proteins present in HeLa cell nuclear extracts interact specifically with Site I sequences.

DOI of Published Version

10.1002/jcb.240580310

Source

J Cell Biochem. 1995 Jul;58(3):372-9. Link to article on publisher's site

Journal/Book/Conference Title

Journal of cellular biochemistry

Related Resources

Link to Article in PubMed

PubMed ID

7593258

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