Topoisomerase from Ustilago maydis forms a covalent complex with single-stranded DNA through a phosphodiester bond to tyrosine. Academic Article uri icon

Overview

abstract

  • Highly purified topoisomerase from Ustilago breaks single-stranded DNA, forming a complex with protein covalently bound to the DNA. Methods used to detect the complexes include a nitrocellulose filter assay, electrophoresis of the DNA-protein complex in agarose gels containing alkali, and isolation of the complex after removal of all but a small oligonucleotide fragment bound to the protein. The linkage of the Ustilago topoisomerase is to the 3' end of the broken strand of DNA. The DNA-protein complex formed is through a phosphodiester bond to tyrosine.

publication date

  • November 18, 1986

Research

keywords

  • Basidiomycota
  • DNA Topoisomerases, Type I
  • DNA, Single-Stranded
  • Tyrosine
  • Ustilago

Identity

Scopus Document Identifier

  • 0023052474

Digital Object Identifier (DOI)

  • 10.1021/bi00371a018

PubMed ID

  • 3026452

Additional Document Info

volume

  • 25

issue

  • 23