Simonin D, Diaz J J, Kindbeiter K, Pernas P, Madjar J J
Immuno-Virologie Moléculaire et Cellulaire, CNRS UMR 30, Faculté de Médecine, Lyon, France.
Electrophoresis. 1995 Jul;16(7):1317-22. doi: 10.1002/elps.11501601216.
The Us11 protein is a true late gene product of herpes simplex virus type 1 (HSV-1), whose exact function is unknown but which exhibits RNA-binding properties and which is phosphorylated on serine residues. In order to determine whether the Us11 protein is phosphorylated by cellular kinase(s) or by virally encoded kinase(s), the Us11 gene has been cloned and transiently expressed in HeLa cells. In addition, HeLa-derived cell lines have been selected for their ability to express Us11 protein constitutively. 32P-Labeling and analysis by two-dimensional electrophoresis of transiently and constitutively expressed Us11 protein demonstrated that, indeed, multiple phosphorylation of the protein occurs in absence of HSV-1 genome expression, indicating that the protein behaves as a natural substrate for cellular kinase(s). In addition, a sequence heterogeneity of the Us11 protein, due to a difference in the number of SPREPR repeats, has been characterized between different strains of HSV-1.
Us11蛋白是单纯疱疹病毒1型（HSV-1）真正的晚期基因产物，其确切功能尚不清楚，但具有RNA结合特性，且在丝氨酸残基上发生磷酸化。为了确定Us11蛋白是由细胞激酶还是病毒编码的激酶磷酸化，已将Us11基因克隆并在HeLa细胞中瞬时表达。此外，已选择HeLa衍生的细胞系，因其具有组成型表达Us11蛋白的能力。对瞬时和组成型表达的Us11蛋白进行32P标记和二维电泳分析表明，在没有HSV-1基因组表达的情况下，该蛋白确实发生了多重磷酸化，这表明该蛋白是细胞激酶的天然底物。此外，由于SPREPR重复序列数量的差异，已在不同的HSV-1毒株之间鉴定出Us11蛋白的序列异质性。
