Papkoff, J. and Nigg, E. A. and Hunter, T.. (1983) The transforming protein of Moloney murine sarcoma virus is a soluble cytoplasmic protein. Cell, Vol. 33, H. 1. pp. 161-172.
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Official URL: http://edoc.unibas.ch/dok/A5249523
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Abstract
The transforming gene, v-mos, of Moloney murine sarcoma virus (M-MuSV) encodes a 37,000-dalton phosphoprotein, p37mos. Since the biochemical function of this protein is unknown, we have determined the subcellular location of p37mos in M-MuSV 124-transformed cells. Using two different methods of cell lysis and fractionation, we found that newly synthesized as well as mature p37mos is a soluble cytoplasmic protein. In agreement with these results, immunofluorescent staining of cells acutely infected with M-MuSV 124, using an antiserum directed against a synthetic v-mos peptide, produced a diffuse cytoplasmic pattern. Gel filtration experiments and glycerol gradient sedimentation analysis suggest that the bulk of p37mos exists as a monomer and is not involved in a specific association with other cellular proteins. These properties of p37mos are different from those of other characterized retroviral transforming proteins.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum 05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Cell Biology (Nigg) |
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UniBasel Contributors: | Nigg, Erich A. |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | Cell Press |
ISSN: | 0092-8674 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
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Identification Number: |
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Last Modified: | 22 Mar 2012 14:19 |
Deposited On: | 22 Mar 2012 13:17 |
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