Poulat F, Girard F, Chevron M P, Gozé C, Rebillard X, Calas B, Lamb N, Berta P
Centre de Recherche de Biochimie Macromoléculaire, CNRS/INSERM, Montpellier, France.
J Cell Biol. 1995 Mar;128(5):737-48. doi: 10.1083/jcb.128.5.737.
We have studied the expression of the human SRY protein (termed p27SRY) in two different cell lines by using specific antibodies. Confocal microscopy enabled us to localize p27SRY precisely in the nucleus in a discrete punctuate pattern. Furthermore, through microinjection experiments, we have demonstrated that the localization of the p27SRY protein into the nucleus was an event involving the NH2-terminal part of the high mobility group (HMG) domain. With the help of several synthetic peptides and various p27SRY mutants, we have characterized a bipartite basic motif in this part of the protein corresponding to a nuclear localization signal. This nuclear localization signal appears to be highly conserved in SRY box- and HMB box-containing proteins, suggesting common properties of nuclear targeting within the HMG box protein family.
我们通过使用特异性抗体,研究了人类SRY蛋白(称为p27SRY)在两种不同细胞系中的表达情况。共聚焦显微镜使我们能够将p27SRY精确地定位在细胞核中,呈离散的点状模式。此外,通过显微注射实验,我们证明了p27SRY蛋白进入细胞核是一个涉及高迁移率族(HMG)结构域NH2末端部分的事件。借助几种合成肽和各种p27SRY突变体,我们在该蛋白的这一部分鉴定出了一个双分型碱性基序,对应于一个核定位信号。这个核定位信号在含SRY盒和HMB盒的蛋白中似乎高度保守,表明HMG盒蛋白家族内核靶向具有共同特性。