Results

RDF/XMLNTriplesTurtleShow queryShare ▶
SubjectPredicateObject
http://purl.uniprot.org/citations/12199906http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12199906http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12199906http://www.w3.org/2000/01/rdf-schema#comment"

Background

Epstein-Barr virus (EBV) infects resting B-lymphocytes and transforms them into immortal proliferating lymphoblastoid cell lines (LCLs) in vitro. The transformed immunoblasts may grow up as immunoblastic lymphomas in immuno-suppressed hosts.

Results

In order to identify cellular protein targets that may be involved in Epstein-Barr virus mediated B-cell transformation, human LCL cDNA library was screened with one of the transformation associated nuclear antigens, EBNA-3 (also called EBNA-3A), using the yeast two-hybrid system. A clone encoding a fragment of a novel human protein was isolated (clone 538). The interaction was confirmed using in vitro binding assays. A full-length cDNA clone (F538) was isolated. Sequence alignment with known proteins and 3D structure predictions suggest that F538 is a novel human uridine kinase/uracil phosphoribosyltransferase. The GFP-F538 fluorescent fusion protein showed a preferentially cytoplasmic distribution but translocated to the nucleus upon co-expression of EBNA-3. A naturally occurring splice variant of F538, that lacks the C-terminal uracil phosphoribosyltransferase part but maintain uridine kinase domain, did not translocate to the nucleus in the presence of EBNA3. Antibody that was raised against the bacterially produced GST-538 protein showed cytoplasmic staining in EBV negative Burkitt lymphomas but gave a predominantly nuclear staining in EBV positive LCL-s and stable transfected cells expressing EBNA-3.

Conclusion

We suggest that EBNA-3 by direct protein-protein interaction induces the nuclear accumulation of a novel enzyme, that is part of the ribonucleotide salvage pathway. Increased intranuclear levels of UK/UPRT may contribute to the metabolic build-up that is needed for blast transformation and rapid proliferation."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.org/dc/terms/identifier"doi:10.1186/1471-2121-3-23"xsd:string
http://purl.uniprot.org/citations/12199906http://purl.org/dc/terms/identifier"doi:10.1186/1471-2121-3-23"xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/author"Klein G."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/author"Klein G."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/author"Sandalova T."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/author"Sandalova T."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/author"Kashuba E."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/author"Kashuba E."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/author"Kashuba V."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/author"Kashuba V."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/author"Szekely L."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/author"Szekely L."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/name"BMC Cell Biol."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/name"BMC Cell Biol."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/pages"23"xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/pages"23"xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/title"Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/title"Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase."xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/volume"3"xsd:string
http://purl.uniprot.org/citations/12199906http://purl.uniprot.org/core/volume"3"xsd:string
▶