The cell-specific transcription factor PTF1 contains two different subunits that interact with the DNA

The cognate sequence of transcription factor PTF1, which plays a key role in pancreas-specific gene expression, has a bipartite organization. Two separate DNA domains, the A and the B boxes, are required for efficient binding of the factor. The structure of PTF1 was elucidated by cross-linking purif...

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Bibliographic Details
Published in:Genes & development 1989-10, Vol.3 (10), p.1613-1624
Main Authors: ROUX, E, STRUBIN, M, HAGENBÜCHLE, O, WELLAUER, P. K
Format: Article
Language:English
Subjects:
560120 - Radiation Effects on Biochemicals, Cells, & Tissue Culture
alpha-Amylases - genetics
ANIMALS
Base Sequence
Biological and medical sciences
BODY
CHEMICAL REACTIONS
CHROMATOGRAPHY
Chromatography, Affinity
CROSS-LINKING
Cross-Linking Reagents - chemical synthesis
Cross-Linking Reagents - metabolism
DIGESTIVE SYSTEM
DNA
DNA - metabolism
DNA Probes
ELECTROMAGNETIC RADIATION
ENDOCRINE GLANDS
Fundamental and applied biological sciences. Psychology
GENE REGULATION
GLANDS
IN VITRO
In Vitro Techniques
MAMMALS
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
MOLECULAR STRUCTURE
NUCLEIC ACIDS
ORGANIC COMPOUNDS
ORGANS
PANCREAS
POLYMERIZATION
Protein Binding - physiology
PROTEINS
RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT
RADIATIONS
RATS
REAGENTS
RODENTS
SEPARATION PROCESSES
TRANSCRIPTION
Transcription Factors - metabolism
Transcription Factors - ultrastructure
Transcription. Transcription factor. Splicing. Rna processing
ULTRAVIOLET RADIATION
Ultraviolet Rays
VERTEBRATES
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Summary:The cognate sequence of transcription factor PTF1, which plays a key role in pancreas-specific gene expression, has a bipartite organization. Two separate DNA domains, the A and the B boxes, are required for efficient binding of the factor. The structure of PTF1 was elucidated by cross-linking purified PTF1 to DNA templates that had been differentially substituted with azido-deoxyuridine (N3.dU). This site-directed UV cross-linking shows that PTF1 contains two DNA-binding proteins, distinct in size and sensitivity to Staphylococcus aureus V8 protease. A 64-kD protein is cross-linked with DNA containing N3.dU substitutions in the A box, and a 48-kD protein is cross-linked with DNA containing N3.dU substitutions in the B box. Both proteins bind simultaneously to the same DNA molecule. The data indicate that PTF1 is a heteromeric oligomer and that its cell-specific DNA-binding potential is the result of a concerted activity of two DNA-binding subunits.
ISSN:0890-9369
1549-5477
DOI:10.1101/gad.3.10.1613