MOLECULAR-CLONING OF THE MICROTUBULE-ASSOCIATED MECHANOCHEMICAL ENZYME DYNAMIN REVEALS HOMOLOGY WITH A NEW FAMILY OF GTP-BINDING PROTEINS
MOLECULAR-CLONING OF THE MICROTUBULE-ASSOCIATED MECHANOCHEMICAL ENZYME DYNAMIN REVEALS HOMOLOGY WITH A NEW FAMILY OF GTP-BINDING PROTEINS
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DOI：
10.1038/347256a0
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发表时间：
1990-09-20
期刊：
影响因子：
64.8
通讯作者：
VALLEE, RB
中科院分区：
文献类型：
--
作者：
OBAR, RA;COLLINS, CA;VALLEE, RB
一种编码大鼠脑动力素D100多肽的互补DNA已被克隆和测序。预测的氨基酸序列包括一个鸟嘌呤核苷酸结合结构域，它与干扰素诱导的抗病毒因子家族（称为MX蛋白）和基本酵母空泡蛋白分选基因VPS1的产物同源。这些关系意味着存在一个新的家庭的GTP酶的生理作用，可能包括微管为基础的运动和蛋白质分选。
A complementary DNA encoding the D100 poly-peptide of rat brain dynamin—a force-producing, microtubule-activated nucleotide triphosphatase—has been cloned and sequenced. The predicted amino acid sequence includes a guanine nucleotide-binding domain that is homologous with those of a family of antiviral factors, inducible by interferon and known as MX proteins, and with the product of the essential yeast vacuolar protein sorting geneVPS1. These relationships imply the existence of a new family of GTPases with physiological roles that may include microtubule-based motility and protein sorting.