猿猴病毒40大T抗原磷酸化位点的代谢周转
Metabolic turnover of phosphorylation sites in simian virus 40 large T antigen.
作者信息
Van Roy F, Fransen L, Fiers W
出版信息
J Virol. 1983 Jan;45(1):442-6. doi: 10.1128/JVI.45.1.442-446.1983.
Abstract
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.
摘要
猴病毒40大T抗原中存在四个磷酸化位点组，它们涉及至少两个丝氨酸和两个苏氨酸残基（范·罗伊等人，《病毒学杂志》45:315 - 331，1983年）。所有磷酸化位点均被发现以离散速率发生修饰和再次去磷酸化，其中磷酸丝氨酸残基的周转率最高。测得的半衰期在3小时（羧基末端磷酸丝氨酸位点）至5.5小时（氨基末端磷酸苏氨酸位点）之间。还研究了四个温度敏感A突变对大T抗原磷酸化的影响。在限制温度下，发现突变大T抗原中羧基末端磷酸丝氨酸的磷酸化特别受损。这些数据强调了后一个磷酸化位点的生理重要性。
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