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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0019351,
umls-concept:C0035547,
umls-concept:C0185117,
umls-concept:C0205263,
umls-concept:C0205282,
umls-concept:C1510411,
umls-concept:C1514562,
umls-concept:C1711351,
umls-concept:C2349975,
umls-concept:C2911684
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pubmed:issue |
18
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pubmed:dateCreated |
1991-10-21
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pubmed:abstractText |
The 1.3-kilobase (kb) Pst I DNA fragment C (Pst I-C) of herpes simplex virus type 2 (HSV-2) morphological transforming region III (mtrIII; map unit 0.562-0.570) encodes part of the N-terminal half of the large subunit of ribonucleotide reductase (RR1; amino acid residues 71-502) and induces the neoplastic transformation of immortalized cell lines. To assess directly the role of these RR1 protein sequences in cell transformation, the Pst I-C fragment was cloned in an expression vector (p91023) containing an adenovirus-simian virus 40 promoter-enhancer to generate recombinant plasmid p9-C. Expression of a protein domain (approximately 65 kDa) was observed in p9-C-transfected COS-7 and Rat2 cells but not in those transfected with plasmid pHC-14 (Pst I-C in a promoterless vector). In Rat2 cells, p9-C induced highly transformed foci at an elevated frequency compared with that of pHC-14. Introduction of translation termination (TAG) condons within the RR1 coding sequence and within all three reading frames inactivated RR1 protein expression from p9-C and reduced its transforming activity to the level seen with the standard pHC-14 construct. Wild-type p9-C specified a protein kinase capable of autophosphorylation. Computer-assisted analysis further revealed significant similarity between regions of mtrIII-specific RR1 and amino acid patterns conserved within the proinsulin precursor family and DNA transposition proteins. These results identify a distinct domain of the HSV-2 RR1 protein involved in the induction of enhanced malignant transformation. In addition, the data indicate that the mtrIII DNA itself can induce basal-level transformation in the absence of protein expression.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-1851753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-215318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-2171197,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-2296575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-2419588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-2539696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-2545912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-2558154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-2835765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-2836266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-2983309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-3001705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-3006067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-3020562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-3039500,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-3154283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-3670292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-6253164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-6277788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1654564-6298276
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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 |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
88
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pubmed:geneSymbol |
mtrIII
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8257-61
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1654564-Amino Acid Sequence,
pubmed-meshheading:1654564-Animals,
pubmed-meshheading:1654564-Cell Transformation, Viral,
pubmed-meshheading:1654564-Cells, Cultured,
pubmed-meshheading:1654564-Cercopithecus aethiops,
pubmed-meshheading:1654564-Cloning, Molecular,
pubmed-meshheading:1654564-DNA, Viral,
pubmed-meshheading:1654564-DNA Mutational Analysis,
pubmed-meshheading:1654564-Genes, Viral,
pubmed-meshheading:1654564-Macromolecular Substances,
pubmed-meshheading:1654564-Molecular Sequence Data,
pubmed-meshheading:1654564-Oncogenes,
pubmed-meshheading:1654564-Protein Kinases,
pubmed-meshheading:1654564-Rats,
pubmed-meshheading:1654564-Ribonucleotide Reductases,
pubmed-meshheading:1654564-Sequence Alignment,
pubmed-meshheading:1654564-Simplexvirus,
pubmed-meshheading:1654564-Viral Structural Proteins
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pubmed:year |
1991
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pubmed:articleTitle |
Enhanced malignant transformation induced by expression of a distinct protein domain of ribonucleotide reductase large subunit from herpes simplex virus type 2.
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pubmed:affiliation |
Viral Carcinogenesis Laboratories, Linus Pauling Institute of Science and Medicine, Palo Alto, CA 94306.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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