核 ATP 酶/腺苷酸激酶 hCINAP 被招募到 RNA pol.II 抑制时产生的核仁周帽中。
The nuclear ATPase/adenylate kinase hCINAP is recruited to perinucleolar caps generated upon RNA pol.II inhibition.
机构信息
Department of Biological Sciences, University of Cyprus and Cyprus Institute of Neurology and Genetics, P.O. Box 20537, 1678 Nicosia, Cyprus.
出版信息
FEBS Lett. 2010 Nov 19;584(22):4559-64. doi: 10.1016/j.febslet.2010.10.044. Epub 2010 Oct 26.
hCINAP is an atypical nucleoplasmic enzyme, combining structural features of adenylate kinases and ATPases, which exhibits dual enzymatic activity. It interacts with the Cajal Body marker coilin and its level of expression and enzymatic activity influence Cajal Body numbers. Here we show that upon specific transcriptional inhibition of RNA pol.II, hCINAP segregates in perinuclear caps identified as Dark Nucleolar Caps (DNCs). These are distinct from perinucleolar caps where coilin and fibrillarin (both Cajal Body components) accumulate. In DNCs, hCINAP co-localizes with Paraspeckle Protein (PSP1) and also co-segregates with PSP1, and not coilin, in nuclear and nucleolar foci upon UV irradiation.
hCINAP 是一种非典型核质酶，结合了腺苷酸激酶和 ATP 酶的结构特征，具有双重酶活性。它与 Cajal 体标记 coilin 相互作用，其表达水平和酶活性影响 Cajal 体的数量。在这里，我们表明，在特定的 RNA pol.II 转录抑制后，hCINAP 会在核周帽中分离出来，这些帽被确定为暗核仁帽（DNCs）。这些帽与 coilin 和核仁小纤维蛋白（Cajal 体成分）积累的核周帽不同。在 DNCs 中，hCINAP 与 Paraphrase 蛋白（PSP1）共定位，并且在 UV 照射后，在核和核仁焦点中，hCINAP 与 PSP1 共同分离，而不是 coilin。
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