植物DNA拓扑异构酶I可被人类抗Scl - 70血清自身抗体识别并抑制。

Plant DNA topoisomerase I is recognized and inhibited by human Scl-70 sera autoantibodies.

作者信息

Agris P F, Parks R, Bowman L, Guenther R H, Kovacs S A, Pelsue S

机构信息

Department of Biochemistry, North Carolina State University, Raleigh 27695-7622.

出版信息

Exp Cell Res. 1990 Aug;189(2):276-9. doi: 10.1016/0014-4827(90)90247-8.

DOI:10.1016/0014-4827(90)90247-8

PMID:2164485

Abstract

Type I topoisomerases (EC 5.99.1.2) are those enzymes capable of relaxing negatively supercoiled DNA without the need for ATP. The central role played by these enzymes in cell function suggests that the structure of type I topoisomerases may be highly conserved in eukaryotic cells. However, the extent of the conservation among eukaryotes is unknown. Human DNA topoisomerase I is an autoimmune antigen (Scl-70) of scleroderma patients. We have found that the autoimmune antibodies in human Scl-70 sera recognize protein from various plants, and these proteins display DNA relaxation function. In addition, Scl-70 antibodies were able to inhibit enzymatic activity of plant topoisomerase I. Therefore, the immunological cross-reactivity of the plant topoisomerase with human antibodies demonstrates that, despite divergence of eukaryotic organisms, these plant and animal enzymes retain structurally similar enzymatic features.

摘要

I型拓扑异构酶（EC 5.99.1.2）是那些能够在不需要ATP的情况下松弛负超螺旋DNA的酶。这些酶在细胞功能中所起的核心作用表明，I型拓扑异构酶的结构在真核细胞中可能高度保守。然而，真核生物之间的保守程度尚不清楚。人DNA拓扑异构酶I是硬皮病患者的自身免疫抗原（Scl-70）。我们发现，人类Scl-70血清中的自身免疫抗体能识别来自各种植物的蛋白质，并且这些蛋白质具有DNA松弛功能。此外，Scl-70抗体能够抑制植物拓扑异构酶I的酶活性。因此，植物拓扑异构酶与人类抗体的免疫交叉反应表明，尽管真核生物存在差异，但这些植物和动物酶在结构上保留了相似的酶学特征。