Kasbekar Durgadas P
Centre for DNA Fingerprinting and Diagnostics, Uppal, Hyderabad 500 039, India,
J Biosci. 2018 Jun;43(2):235-237.
The vertebrate inner nuclear membrane protein, lamin B receptor, has an N-terminal ~200 residue nucleoplasmic domain (NTD), and a ~420 residue C-terminal domain (CTD) that anchors the NTD to the INM. Chen (2016) showed the NTD interacts with Xist long noncoding RNA to effect X chromosome inactivation in female mammals. Tsai (2016) showed the CTD has sterol reductase activity that is essential for viability. And Nikolakaki (2017) proposed a model to interconnect these disparate functions of this chimeric protein. It amuses me now to think back to 24 years ago, when I was concerned that these domains might have come together in a cloning artifact.
脊椎动物的内核膜蛋白——核纤层蛋白B受体,有一个N端约200个残基的核质结构域(NTD),以及一个约420个残基的C端结构域(CTD),该结构域将NTD锚定在内核膜上。Chen(2016年)表明,NTD与Xist长链非编码RNA相互作用,以实现雌性哺乳动物的X染色体失活。Tsai(2016年)表明,CTD具有对生存能力至关重要的固醇还原酶活性。Nikolakaki(2017年)提出了一个模型,将这种嵌合蛋白的这些不同功能联系起来。现在回想24年前,我当时担心这些结构域可能是在克隆人工制品中组合在一起的,这让我觉得很有趣。