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PMID: 1570345 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 89 ·No. 9 ·1992-05-01 ·Pages 4178-82

Dworetzky SI, Wright KL, Fey EG, Penman S, Lian JB, Stein JL, Stein GS

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.

MeSH Terms
Base Sequence Binding Sites Consensus Sequence Cross-Linking Reagents DNA-Binding Proteins/chemistry,metabolism HeLa Cells Histones/genetics Humans Molecular Sequence Data Molecular Weight Nuclear Matrix/ultrastructure Nuclear Proteins/chemistry,metabolism Promoter Regions, Genetic Restriction Mapping
Chemicals
Cross-Linking Reagents DNA-Binding Proteins Histones Nuclear Proteins
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Dworetzky S I
Department of Cell Biology, University of Massachusetts Medical Center, Worcester 01655.
Wright K L
Fey E G
Penman S
Lian J B
Stein J L
Stein G S
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.89.9.4178
Published
1992-05-01
Pages
4178-82
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC525656
Subset
IM
Grants
NIAMS NIH HHS · AR39588 · United States
NIGMS NIH HHS · GM32010 · United States
External Links
PubMed source DOI: 10.1073/pnas.89.9.4178 PMC Full Text View journal details
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