Agutter P S, Suckling K E
Biochim Biophys Acta. 1982 Sep 27;698(3):223-9. doi: 10.1016/0167-4781(82)90151-8.
The binding of colchicine to nuclear envelopes was studied in order to elucidate the mechanism whereby this compound inhibits nucleocytoplasmic RNA transport. The results suggest that a single class of colchicine-binding site (dissociation constant=approx. 0.7 mM, concentration=approx. 330 nmol colchicine/mg protein) is localised in the nuclear periphery (pore-lamina) and that binding to these sites effects a constriction of the pore-complexes with concomitant inhibition of RNA egress and disordering of the nuclear membrane phospholipid bilayers.
为了阐明秋水仙碱抑制核质RNA转运的机制,对秋水仙碱与核被膜的结合进行了研究。结果表明,一类秋水仙碱结合位点(解离常数约为0.7 mM,浓度约为330 nmol秋水仙碱/ mg蛋白质)定位于核周边(孔板层),与这些位点的结合会导致孔复合体收缩,同时抑制RNA流出,并使核膜磷脂双层紊乱。