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首页> 外文期刊>Journal of Virology >Posttranslational processing of the Epstein-Barr virus-encoded p63/LMP protein.
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Posttranslational processing of the Epstein-Barr virus-encoded p63/LMP protein.

机译：Epstein-BARR病毒编码P63 / LMP蛋白的后翻译加工。

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In this paper we describe the posttranslational processing of the p63/LMP (latent membrane protein) encoded by Epstein-Barr virus in transformed B cells. Specifically, we show that after synthesis, free LMP disappeared with a half-life of about 0.5 h. This was caused by the association of LMP with an insoluble complex. All detectable LMP in the plasma membrane was insoluble. This interaction was resistant to nondenaturing detergents but readily dissociated with 8 M urea or by boiling in 0.5% sodium dodecyl sulfate, suggesting that LMP may be associated with cytoskeletal elements. Most of the Nonidet P-40-insoluble LMP was phosphorylated (ppLMP) primarily on serine but also on threonine residues. No phosphotyrosine was detected. Furthermore, greater than 90% of the ppLMP resided in the Nonidet P-40-insoluble fraction, suggesting a strong correlation between complexing and phosphorylation. Additionally, ppLMP was found to be associated with a 53,000-molecular-weight phosphoprotein (pp53) of unknown origin. Finally, LMP turned over extremely rapidly, with a half-life of about 2 h. Taken together, these properties suggest that although LMP falls broadly within the category of phosphorylated, cytoskeleton-associated oncoproteins, it is nevertheless clearly different from any previously described member of this family.
机译：在本文中，我们描述了在转化的B细胞中由Epstein-Barr病毒编码的P63 / LMP（潜膜蛋白）的发生后处理。具体而言，我们表明，在合成之后，自由LMP消失，半衰期为约0.5小时。这是由LMP与不溶性复合物的关联引起的。血浆膜中的所有可检测的LMP不溶于溶解。该相互作用耐抗体洗涤剂，但易于用8M尿素或煮沸在0.5％十二烷基硫酸钠中的溶解，表明LMP可以与细胞骨骼元素相关。大多数Nonidet P-40-Insoluble LMP主要是磷酸化（PPLMP），主要用于丝氨酸，而且在苏氨酸残基上。没有检测到磷酸酪氨酸。此外，大于90％的PPLMP在非经济型P-40 - 不溶性分数中留下的PPLMP，表明络合和磷酸化之间的强相关性。另外，发现PPLMP与未知来源的53,000分子量磷蛋白（PP53）相关。最后，LMP非常迅速地转化，半衰期约为2小时。这些特性占据了这些特性，虽然LMP在磷酸化的型细胞骨架类别的类别范围内逐渐下降，但仍然明显不同于该家庭的任何先前描述的成员。

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