Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2000-4-4
pubmed:abstractText
E6 is an oncoprotein implicated in cervical cancers, produced by "high-risk" human papillomaviruses. E6 is thought to promote tumorigenesis by stimulating cellular degradation of the tumour suppressor p53, but it might display other activities. Sequence similarity was recently detected between E6 and endonuclease VII, a protein of phage T4 that recognizes and cleaves four-way DNA junctions. Here, we purified recombinant E6 proteins and demonstrated that high-risk E6 s bind selectively to four-way junctions in a structure-dependent manner. Several residues in the C-terminal zinc-binding domain, the region of E6 similar to endonuclease VII, are necessary for the junction-binding activity. E6 binds to the junction as a monomer. Comparative electrophoresis shows that E6-bound junctions migrate in an extended square conformation. Magnesium inhibits the electrophoretic migration of the complexes but does not seem to influence their formation at equilibrium. This work is the first demonstration of specific binding of purified active E6 to a well-characterized DNA ligand, and suggests new modes of action of E6 in oncogenesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
296
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1189-203
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10698626-Amino Acid Sequence, pubmed-meshheading:10698626-Binding Sites, pubmed-meshheading:10698626-DNA, pubmed-meshheading:10698626-DNA Probes, pubmed-meshheading:10698626-DNA-Binding Proteins, pubmed-meshheading:10698626-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:10698626-Endodeoxyribonucleases, pubmed-meshheading:10698626-Magnesium, pubmed-meshheading:10698626-Molecular Sequence Data, pubmed-meshheading:10698626-Mutation, pubmed-meshheading:10698626-Nucleic Acid Conformation, pubmed-meshheading:10698626-Oncogene Proteins, Viral, pubmed-meshheading:10698626-Papillomaviridae, pubmed-meshheading:10698626-Protein Structure, Quaternary, pubmed-meshheading:10698626-Protein Structure, Tertiary, pubmed-meshheading:10698626-Recombinant Fusion Proteins, pubmed-meshheading:10698626-Sequence Homology, Amino Acid, pubmed-meshheading:10698626-Static Electricity, pubmed-meshheading:10698626-Substrate Specificity, pubmed-meshheading:10698626-Thermodynamics, pubmed-meshheading:10698626-Tumor Suppressor Protein p53, pubmed-meshheading:10698626-Zinc
pubmed:year
2000
pubmed:articleTitle
HPV oncoprotein E6 is a structure-dependent DNA-binding protein that recognizes four-way junctions.
pubmed:affiliation
Laboratoire d'Immunotechnologie, UPRES 1329, Ecole Superieure de Biotechnologie de Strasbourg, Illkirch, 67400, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't