A DNA-binding protein from Ustilago maydis prefers duplex DNA without chain interruptions. Academic Article uri icon

Overview

abstract

  • Using a nitrocellulose filter binding assay, we have partially purified a protein from mitotic cells of Ustilago maydis that binds preferentially to covalently closed circular duplex DNA. DNA containing single- or double-strand breaks is bound poorly by the protein. Once formed, the DNA-protein complex is stable, resisting dissociation in high salt. However, when a DNA strand is broken, the complex appears to dissociate. The protein binds equally well to form I DNA of phi X174 or the plasmid pBR322, but has a higher affinity for a hybrid plasmid containing a cloned region of Drosophila melanogaster satellite DNA.

publication date

  • April 1, 1983

Research

keywords

  • DNA Helicases
  • DNA, Satellite

Identity

PubMed Central ID

  • PMC368576

Scopus Document Identifier

  • 0020537656

PubMed ID

  • 6304499

Additional Document Info

volume

  • 3

issue

  • 4