Affordable Access

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

Authors
  • Agris, P F
  • Parks, R
  • Bowman, L
  • Guenther, R H
  • Kovacs, S A
  • Pelsue, S
Type
Published Article
Journal
Experimental cell research
Publication Date
Aug 01, 1990
Volume
189
Issue
2
Pages
276–279
Identifiers
PMID: 2164485
Source
Medline
License
Unknown

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.

Report this publication

Statistics

Seen <100 times