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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2004-2-12
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pubmed:abstractText |
The avian Rev-T retrovirus encodes the oncoprotein v-Rel, a member of the Rel/nuclear factor (NF)-kappaB transcription factor family. The aggressive oncogenic potential of v-Rel has arisen from multiple mutations within the coding sequence of the avian cellular protein c-Rel. In this study, using quantitative biochemical experiments, we have tested the role of a limited set of alterations between v-Rel and c-Rel located within the Rel homology region (RHR) of the family that might confer functional differences. Our results show that only a set of six mutations within the RHR of v-Rel are responsible for its ability to bind to a broad spectrum of kappaB-DNA that are normally regulated by distinct NF-kappaB dimers. We also observe that both v-Rel homodimer and p50/v-Rel heterodimer bind IkappaBalpha weakly compared to other cellular Rel/NF-kappaB dimers with transcription activation potential. We suggest that the ability of v-Rel homodimer to deregulate subunit-specific gene expression and its ability to evade IkappaB inhibition are crucial to its strong oncogenic potential.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0950-9232
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1229-38
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14961076-Animals,
pubmed-meshheading:14961076-Base Sequence,
pubmed-meshheading:14961076-Chickens,
pubmed-meshheading:14961076-Cloning, Molecular,
pubmed-meshheading:14961076-DNA,
pubmed-meshheading:14961076-DNA Primers,
pubmed-meshheading:14961076-Dimerization,
pubmed-meshheading:14961076-Escherichia coli,
pubmed-meshheading:14961076-Humans,
pubmed-meshheading:14961076-I-kappa B Proteins,
pubmed-meshheading:14961076-Mutagenesis, Site-Directed,
pubmed-meshheading:14961076-Mutation,
pubmed-meshheading:14961076-NF-kappa B,
pubmed-meshheading:14961076-Oncogene Proteins v-rel,
pubmed-meshheading:14961076-Proto-Oncogene Proteins c-rel,
pubmed-meshheading:14961076-Recombinant Proteins,
pubmed-meshheading:14961076-Sequence Homology, Nucleic Acid
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pubmed:year |
2004
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pubmed:articleTitle |
Discreet mutations from c-Rel to v-Rel alter kappaB DNA recognition, IkappaBalpha binding, and dimerization: implications for v-Rel oncogenicity.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of California, San Deigo, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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