Alkylation Interference Identifies Essential DNA Contacts for Sequence- Specific Binding of the Eukaryotic Transcription Factor C/EBP

Transcriptional regulators containing a "leucine zipper" and a flanking basic domain belong to a recently identified class of DNA-binding proteins. We have mapped the essential DNA contacts of one member of this group, the eukaryotic transcription factor C/EBP. Methylation and ethylation i...

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Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 87; no. 10; pp. 3992 - 3996
Main Authors Nye, Julie A., Graves, Barbara J.
Format Journal Article
LanguageEnglish
Published Washington, DC National Academy of Sciences of the United States of America 01.05.1990
National Acad Sciences
Subjects
Alkylation
Base Sequence
Binding Sites
Biological and medical sciences
CCAAT-Enhancer-Binding Proteins
Dimers
DNA
DNA, Viral - drug effects
DNA, Viral - metabolism
DNA-Binding Proteins - metabolism
Dyadic relations
Ethylnitrosourea - pharmacology
Fundamental and applied biological sciences. Psychology
Gels
Methylation
Models, Molecular
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Nuclear Proteins - metabolism
Nucleic Acid Conformation
Nucleotides
Phosphates
Promoter Regions, Genetic
Repetitive Sequences, Nucleic Acid
Restriction Mapping
Sarcoma Viruses, Murine - genetics
Symmetry
Transcription Factors - metabolism
Transcription. Transcription factor. Splicing. Rna processing
Eucaryote
Radiolabelling
Gel electrophoresis
DNA binding protein
Binding site
Transcription factor
Alkylation
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Summary:Transcriptional regulators containing a "leucine zipper" and a flanking basic domain belong to a recently identified class of DNA-binding proteins. We have mapped the essential DNA contacts of one member of this group, the eukaryotic transcription factor C/EBP. Methylation and ethylation interference experiments detected major groove contacts over a full turn of the DNA helix on both an asymmetric and a symmetric C/EBP binding site. The contacts essential for C/EBP binding have two-fold symmetry yet differ significantly from the contacts of other dimeric DNA-binding proteins, including those bearing helix-turn-helix motifs and the type I restriction endonuclease EcoRI.
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ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.87.10.3992