DNA bending is induced in an enhancer by the DNA-binding domain of the bovine papillomavirus E2 protein

The E2 gene of bovine papillomavirus type 1 has been shown to encode a DNA-binding protein and to trans-activate the viral enhancer. We have localized the DNA-binding domain of the E2 protein to the carboxyl-terminal 126 amino acids of the E2 open reading frame. The DNA-binding domain has been expre...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1988-03, Vol.85 (6), p.1826-1830
Main Authors: Moskaluk, C, Bastia, D
Format: Article
Language:English
Subjects:
ADN
Base Sequence
Bending
Binding sites
Biological and medical sciences
BOVINE PAPILLOMAVIRUS
Bovine papillomavirus 1
Coordinate systems
Deoxyribonuclease I - metabolism
DNA
DNA-Binding Proteins - metabolism
Electrophoresis
Enhancer Elements, Genetic
Fundamental and applied biological sciences. Psychology
Gels
GENE
GENES
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Nucleic Acid Conformation
Open reading frames
PAPILLOMAVIRUS BOVIN
Plasmids
PROTEINAS
PROTEINE
PROTEINS
Transcription. Transcription factor. Splicing. Rna processing
Ungulates
Viral Proteins - metabolism
VIRUS DEL PAPILOMA BOVINO
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Summary:The E2 gene of bovine papillomavirus type 1 has been shown to encode a DNA-binding protein and to trans-activate the viral enhancer. We have localized the DNA-binding domain of the E2 protein to the carboxyl-terminal 126 amino acids of the E2 open reading frame. The DNA-binding domain has been expressed in Escherichia coli and partially purified. Gel retardation and DNase I ``footprinting'' on the bovine papillomavirus type 1 enhancer identify the sequence motif ACCN6GGT (in which N = any nucleotide) as the E2 binding site. Using electrophoretic methods we have shown that the DNA-binding domain changes conformation of the enhancer by inducing significant DNA bending.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.85.6.1826