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人拓扑异构酶I氨基末端的作用。

A role for the amino terminus of human topoisomerase I.

作者信息

Haluska P, Rubin E H

机构信息

Department of Pharmacology, Robert Wood Johnson Medical School, Cancer Institute of New Jersey, University of Medicine, New Brunswick 08901, USA.

出版信息

Adv Enzyme Regul. 1998;38:253-62. doi: 10.1016/s0065-2571(97)00008-3.

Abstract

These studies indicate that SV40T antigen binds the amino terminus of human top1 both in vitro and in vivo. Additional in vitro data suggest that the interaction between these two proteins does not require DNA as an intermediary. Taken together with the finding that the amino terminus of top 1 binds the putative helicase nucleolin, these results implicate helicase binding as a general function of the amino terminus of human top1. Binding of top1 by helicases may be important in the management of structural alterations in DNA produced by helicases. The potential importance of helicase-topoisomerase interactions has been highlighted by recent data indicating that the protein defective in Bloom's syndrome is a helicase with a yeast homologue that is known to bind topoisomerases.

摘要

这些研究表明,SV40T抗原在体外和体内均与人top1的氨基末端结合。更多体外实验数据表明,这两种蛋白质之间的相互作用不需要DNA作为中介。结合top1氨基末端与假定解旋酶核仁素结合的发现,这些结果表明解旋酶结合是人类top1氨基末端的一般功能。解旋酶与top1的结合可能在处理解旋酶产生的DNA结构改变中起重要作用。解旋酶与拓扑异构酶相互作用的潜在重要性已被最近的数据所强调,这些数据表明,布卢姆综合征中存在缺陷的蛋白质是一种解旋酶,其酵母同源物已知可与拓扑异构酶结合。

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