Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment.
Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment.
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NDP52 的分子特征，NDP52 是核结构域 10 的一种新型蛋白质，在病毒感染和干扰素治疗后重新分布。
DOI：
10.1083/jcb.130.1.1
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发表时间：
1995-07
期刊：
影响因子：
--
通讯作者：
Frey J
中科院分区：
文献类型：
--
作者：
Korioth F;Gieffers C;Maul GG;Frey J
核结构域（ND）10也被描述为POD或Kr体，参与急性早幼粒细胞白血病的发展和病毒-宿主相互作用。使用各种人自身免疫血清和单克隆抗体的免疫荧光分析显示ND 10的典型点状核染色，表明该结构由几种蛋白质组成。两个ND 10蛋白，Sp100和PML的遗传特征，并显示与几个转录因子的同源性。在这里，我们描述了NDP 52，ND 10的另一种新蛋白。我们提出了一种新的mAb C8 A2，其特异性地识别NDP 52。使用该mAb的免疫荧光分析显示出典型的核点染色，如ND 10所述。相应cDNA的分离和测序显示NDP 52的预测分子量为52 kD。推导的氨基酸序列具有一个扩展的中央卷曲螺旋域含有亮氨酸拉链基序。NDP 52的COOH末端显示出与LIM结构域的同源性，LIM结构域最近被描述为介导蛋白质相互作用，这使得NDP 52似乎是介导ND 10蛋白之间相互作用的合适候选者。在体内，NDP 52在所分析的所有人类组织中转录。此外，我们发现NDP 52与ND 10蛋白PML共定位，并可在病毒感染和干扰素治疗后重新分布。这些数据表明，ND 10蛋白在病毒的生命周期中发挥着重要作用。
The nuclear domain (ND)10 also described as POD or Kr bodies is involved in the development of acute promyelocytic leukemia and virus- host interactions. Immunofluorescence analysis using a variety of human autoimmune sera and monoclonal antibodies showed a typical dot like nuclear staining for ND10, suggesting that this structure consists of several proteins. Two of the ND10 proteins, Sp100 and PML are genetically characterized and show homology with several transcription factors. Here we describe NDP52, an additional novel protein of the ND10. We raised a new mAb C8A2, that specifically recognizes NDP52. Immunofluorescence analysis using this mAb showed a typical nuclear dot staining as it was described for ND10. Isolation and sequencing of the corresponding cDNA revealed that NDP52 has a predicted molecular mass of 52 kD. The deduced amino acid sequence exhibits an extended central coiled coil domain containing a leucine zipper motif. The COOH terminus of NDP52 shows homology with LIM domains, that have recently been described to mediate protein interactions, which let NDP52 appear as a suitable candidate for mediating interactions between ND10 proteins. In vivo, NDP52 is transcribed in all human tissues analyzed. Furthermore, we show that NDP52 colocalizes with the ND10 protein PML and can be redistributed upon viral infection and interferon treatment. These data suggest that ND10 proteins play an important role in the viral life cycle.