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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Oliver, D. B. Benjamin, T. L. Carmichael, G. G. Dorsky, D. I. Schaffhausen, B. S. |
| Abstract | We have constructed a transformation-defective polyoma virus mutant (Py 1387-T) that directs the synthesis of a normal small tumor antigen, a functional large tumor antigen, and a truncated (51,000-dalton) middle-sized tumor (mT) antigen that lacks 37 amino acids at its COOH terminus. The shortened mT polypeptide is missing the hydrophobic 'tail' thought to be responsible for the anchorage of this protein into the plasma membrane and is in fact in cytosol fractions. This truncated mT polypeptide is inactive in an in vitro protein kinase assay and is altered in its phosphorylation in vivo. Mutant 1387-T differs from wild-type virus in having a T.A base pair instead of a C.G base at nucleotide position 1387. This change was introduced into viral DNA by using a synthetic undecanucleotide as a specific mutagen. Wild-type polyoma DNA was rendered single stranded by molecular cloning into coliphage M13. The oligonucleotide, which hybridizes with a mismatch at the site to be altered, was used to prime the synthesis of double-stranded closed circular DNA. Progeny recombinant phage were screened by DNA sequence analysis for the desired base change. The polyoma mutant was reconstructed from recombinant phage replicative form DNA molecules containing the mutation. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 11 |
| Volume Number | 79 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1982-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Antigens, Viral Physiology Cell Transformation, Viral Polyomavirus Protein Kinases Metabolism Animals Antigens, Viral, Tumor Cell Membrane Cells, Cultured Cytoplasm DNA, Recombinant Mice Mutation Phosphotyrosine Immunology Structure-Activity Relationship Tyrosine Analogs & Derivatives Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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