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PMID: 3601664 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Identification of proteins interacting with the enhancer of human U2 small nuclear RNA genes.

Nucleic acids research ·Vol. 15 ·No. 13 ·1987-07-10 ·Pages 4997-5016

Janson L, Bark C, Pettersson U

Abstract

Protein/DNA interactions in the human U2 RNA gene enhancer have been characterized by DNase I footprint and DMS methylation protection analyses. Nuclear factors present in both HeLa and B cell extracts have been shown to protect an approximately 70 bp region from DNase I digestion. DMS and DNase I footprint competition studies demonstrated that the entire footprint can be accounted for by interactions with two previously identified transcription factors. One of these recognizes the so called octanucleotide-motif ATGCAAAT (transcription factor IgNF-A) which has been shown to be essential for transcription. The other is the transcription factor Sp1 which binds to three target sequences located adjacent to the octameric motif. The Sp1 interactions appear to be required for full transcriptional activity. No differences in the DNase I footprint patterns or in the DMS methylation protections were observed when nuclear extracts from HeLa cells, two different B cell lines, or from the adenovirus-transformed 293 cell line were compared.

MeSH Terms
Base Sequence Cell Nucleus/metabolism Deoxyribonuclease I Enhancer Elements, Genetic Genes Genes, Regulator HeLa Cells/metabolism Humans Nucleotide Mapping RNA, Small Nuclear/genetics Transcription Factors/metabolism
Chemicals
RNA, Small Nuclear Transcription Factors Deoxyribonuclease I
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Janson L
Bark C
Pettersson U
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34 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/15.13.4997
Published
1987-07-10
Pages
4997-5016
Language
English
Region
England
NLM ID
0411011
PMCID
PMC305943
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/15.13.4997 PMC Full Text View journal details
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