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A DNA-binding protein from Ustilago maydis prefers duplex DNA without chain interruptions.

TitleA DNA-binding protein from Ustilago maydis prefers duplex DNA without chain interruptions.
Publication TypeJournal Article
Year of Publication1983
AuthorsRusche JR, Holloman WK
JournalMol Cell Biol
Volume3
Issue4
Pagination605-12
Date Published1983 Apr
ISSN0270-7306
KeywordsBinding Sites, DNA Helicases, DNA, Satellite, DNA-Binding Proteins, Fungi, Protein Binding, Structure-Activity Relationship
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.

Alternate JournalMol. Cell. Biol.
PubMed ID6304499
PubMed Central IDPMC368576
Grant ListGM 27103 / GM / NIGMS NIH HHS / United States

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