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Cellular proteins which can specifically associate with simian virus 40 small t antigen.
When crude, radiolabeled extracts of various cells were applied to homogeneous simian virus 40 small t antigen-Sepharose adsorbents, three cell proteins (57, 32, and 20 kilodaltons [kDa]) bound specifically. Each also bound to an insoluble, truncated t derivative composed of the COOH-terminal 123 re...
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1986
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pubmed-2532422003-12-01 Cellular proteins which can specifically associate with simian virus 40 small t antigen. Murphy, C I Bikel, I Livingston, D M J Virol Research Article When crude, radiolabeled extracts of various cells were applied to homogeneous simian virus 40 small t antigen-Sepharose adsorbents, three cell proteins (57, 32, and 20 kilodaltons [kDa]) bound specifically. Each also bound to an insoluble, truncated t derivative composed of the COOH-terminal 123 residues of the protein. The binding of these proteins was greatly inhibited after reduction and alkylation of the t ligand. Therefore, some element of native conformation, but not all of the primary structure of t, is necessary for this binding property, which may constitute a discrete, in vitro biochemical function of this protein. Results of cell fractionation experiments suggested that the 57- and 32-kDa proteins are nonnuclear cell constituents, whereas the 20-kDa protein was closely associated with a detergent-washed nuclear fraction. Specific immunoblotting and comparative partial proteolytic digestion analyses indicated that the 57-kDa protein is tubulin, a major component of the cytoskeleton. In this regard, t and tubulin were observed to coimmunoprecipitate from crude cell extracts after incubation with monospecific anti-t antibody. Therefore, it is possible that t and tubulin interact in vivo. 1986-09 /pmc/articles/PMC253242/ /pubmed/3016331 Text en |
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US National Library of Medicine |
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PubMed Central |
| language |
en |
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Article |
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Research Article |
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Research Article Murphy, C I Bikel, I Livingston, D M Cellular proteins which can specifically associate with simian virus 40 small t antigen. |
| description |
When crude, radiolabeled extracts of various cells were applied to homogeneous simian virus 40 small t antigen-Sepharose adsorbents, three cell proteins (57, 32, and 20 kilodaltons [kDa]) bound specifically. Each also bound to an insoluble, truncated t derivative composed of the COOH-terminal 123 residues of the protein. The binding of these proteins was greatly inhibited after reduction and alkylation of the t ligand. Therefore, some element of native conformation, but not all of the primary structure of t, is necessary for this binding property, which may constitute a discrete, in vitro biochemical function of this protein. Results of cell fractionation experiments suggested that the 57- and 32-kDa proteins are nonnuclear cell constituents, whereas the 20-kDa protein was closely associated with a detergent-washed nuclear fraction. Specific immunoblotting and comparative partial proteolytic digestion analyses indicated that the 57-kDa protein is tubulin, a major component of the cytoskeleton. In this regard, t and tubulin were observed to coimmunoprecipitate from crude cell extracts after incubation with monospecific anti-t antibody. Therefore, it is possible that t and tubulin interact in vivo. |
| author |
Murphy, C I Bikel, I Livingston, D M |
| author_facet |
Murphy, C I Bikel, I Livingston, D M |
| author_sort |
Murphy, C I |
| title |
Cellular proteins which can specifically associate with simian virus 40 small t antigen. |
| title_short |
Cellular proteins which can specifically associate with simian virus 40 small t antigen. |
| title_full |
Cellular proteins which can specifically associate with simian virus 40 small t antigen. |
| title_fullStr |
Cellular proteins which can specifically associate with simian virus 40 small t antigen. |
| title_full_unstemmed |
Cellular proteins which can specifically associate with simian virus 40 small t antigen. |
| title_sort |
cellular proteins which can specifically associate with simian virus 40 small t antigen. |
| publishDate |
1986 |
| url |
https://ncbi.nlm.nih.gov/pmc/articles/PMC253242/ https://ncbi.nlm.nih.gov/pubmed/3016331 |
| _version_ |
1759049643063246848 |