鉴定核定位序列介导的与核膜结合所需的胞质因子。
Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope.
作者信息
Adam E J, Adam S A
机构信息
Department of Cell, Molecular and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611.
出版信息
J Cell Biol. 1994 May;125(3):547-55. doi: 10.1083/jcb.125.3.547.
Abstract
Nuclear protein import can be separated into two distinct steps: binding to the nuclear pore complex followed by translocation to the nuclear interior. A previously identified nuclear location sequence (NLS) receptor and a 97-kD protein purified from bovine erythrocytes reconstitute the binding step in a permeabilized cell assay. Binding to the envelope is specific for a functional SV-40 large T antigen NLS and is not ATP or temperature dependent. Modification of p97 with N-ethylmaleimide (NEM) decreases binding to the pore, but interestingly, NEM treatment of the NLS receptor does not. Nuclear envelope binding is inhibited by wheat germ agglutinin suggesting a possible mechanism for the inhibition of transport by the lectin.
摘要
核蛋白导入可分为两个不同步骤
与核孔复合体结合，随后转运至核内。先前鉴定出的核定位序列（NLS）受体和从牛红细胞中纯化的一种97-kD蛋白，在通透细胞试验中重建了结合步骤。与核膜的结合对功能性SV-40大T抗原NLS具有特异性，且不依赖于ATP或温度。用N-乙基马来酰亚胺（NEM）修饰p97会降低与核孔的结合，但有趣的是，用NEM处理NLS受体则不会。麦胚凝集素可抑制核膜结合，这提示了凝集素抑制转运的一种可能机制。
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