Metabolic turnover of phosphorylation sites in simian virus 40 large T antigen.
AUTOR(ES)
Van Roy, F
RESUMO
Four (groups of) phosphorylation sites exist in the large T antigen of simian virus 40, and they involve at least two serine and two threonine residues (Van Roy et al. J. Virol. 45:315-331, 1983). All the phosphorylation sites were found to be modified and again dephosphorylated at discrete rates, with phosphoserine residues having the highest turnover rate. The measured half-lives ranged between 3 h (for the carboxy-terminal phosphoserine site) and 5.5 h (for the amino-terminal phosphothreonine site). The influence of four temperature-sensitive A mutations on phosphorylation of large T antigen was also examined. At restrictive temperature, phosphorylation of the carboxy-terminal phosphoserine in mutated large T antigen was found to be particularly impaired. These data emphasize the physiological importance of the latter phosphorylation site.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=256427Documentos Relacionados
- Improved localization of phosphorylation sites in simian virus 40 large T antigen.
- Antigenic binding sites of monoclonal antibodies specific for simian virus 40 large T antigen.
- Phosphorylation of threonine in the proline-rich carboxy-terminal region of simian virus 40 large T antigen.
- Use of simian virus 40 large T-beta-galactosidase fusion proteins in an immunochemical analysis of simian virus 40 large T antigen.
- The zinc finger region of simian virus 40 large T antigen.