GSBS Student Publications

Title

Nuclear matrix association of multiple sequence-specific DNA binding activities related to SP-1, ATF, CCAAT, C/EBP, OCT-1, and AP-1

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Cell Biology

Date

8-24-1993

Document Type

Article

Medical Subject Headings

Activating Transcription Factors; Animals; Base Sequence; Blood Proteins; CCAAT-Enhancer-Binding Proteins; DNA-Binding Proteins; Hela Cells; Host Cell Factor C1; Humans; Molecular Sequence Data; Nuclear Matrix; Nuclear Proteins; Octamer Transcription Factor-1; Oligodeoxyribonucleotides; Osteosarcoma; Proto-Oncogene Proteins c-jun; Rats; Substrate Specificity; Transcription Factors; Tumor Cells, Cultured

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The association of DNA binding proteins with the nuclear matrix may be related to a functional role of this subcellular structure in chromatin organization and gene regulation. In this study, nuclear matrix preparations from human HeLa S3 cervical carcinoma and rat ROS 17/2.8 osteosarcoma cells were assayed for the presence of DNA binding activities using consensus binding sequences of well-characterized transcription factors as probes. Competition analysis shows that each probe interacts with different nuclear matrix proteins in a sequence-specific manner and that DNA binding activities related to or identical with SP-1, ATF, CCAAT, C/EBP, OCT-1, and AP-1 are present in the nuclear matrix fraction of different cell types. Comparison of the relative abundance of these transcription factor binding activities in nuclear matrix and nonmatrix nuclear fractions suggests that the distribution between these two fractions is cell type specific, cell growth dependent, or independent of these biological parameters. These results are consistent with the postulated role of the nuclear matrix in transcriptional regulation of gene expression.

Rights and Permissions

Citation: Biochemistry. 1993 Aug 24;32(33):8397-402.

Related Resources

Link to Article in PubMed

Journal Title

Biochemistry

PubMed ID

8357791