GSBS Student Publications

Title

Sequence-specific DNA-binding proteins are components of a nuclear matrix-attachment site

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Cell Biology

Date

5-1-1992

Document Type

Article

Medical Subject Headings

Base Sequence; Binding Sites; Consensus Sequence; Cross-Linking Reagents; DNA-Binding Proteins; Hela Cells; Histones; Humans; Molecular Sequence Data; Molecular Weight; Nuclear Matrix; Nuclear Proteins; Promoter Regions (Genetics); Restriction Mapping

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

We have identified a nuclear matrix-attachment region within an upstream element of a human H4 histone gene promoter. Nuclear matrix proteins, isolated and solubilized from HeLa S3 cells, were found to interact with sequence specificity at this matrix-attachment region. Several types of assays for protein-DNA interaction showed that the minimal sequence for the nuclear matrix protein-DNA interaction was 5'-TGACGTCCATG-3'; the underlined region corresponds to the core consensus sequence for ATF transcription factor binding. Two proteins with molecular masses of 43 and 54 kDa were identified by UV-crosslinking analysis as integral components of this protein-DNA complex. The molecular masses of these proteins and the ATF-binding site consensus sequence suggest that these proteins are members of the ATF family. Our results provide direct evidence for nuclear matrix localization of sequence-specific DNA-binding factors for an actively transcribed gene. The proximity of a strong positive transcriptional regulatory element to the matrix-attachment region of this gene suggests that the nuclear matrix may serve to localize and concentrate trans-acting factors that facilitate regulation of gene expression.

Rights and Permissions

Citation: Proc Natl Acad Sci U S A. 1992 May 1;89(9):4178-82.

Related Resources

Link to article in PubMed

Journal Title

Proceedings of the National Academy of Sciences of the United States of America

PubMed ID

1570345