For COVID-19 vaccine updates, please review our information guide. For patient eligibility and scheduling availability, please visit VaccineTogetherNY.org.

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

TitleTopoisomerase from Ustilago maydis forms a covalent complex with single-stranded DNA through a phosphodiester bond to tyrosine.
Publication TypeJournal Article
Year of Publication1986
AuthorsBrougham MJ, Rowe TC, Holloman WK
JournalBiochemistry
Volume25
Issue23
Pagination7362-8
Date Published1986 Nov 18
ISSN0006-2960
KeywordsBasidiomycota, Binding Sites, DNA Topoisomerases, Type I, DNA, Single-Stranded, Kinetics, Protein Binding, Substrate Specificity, Tyrosine, Ustilago
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.

Alternate JournalBiochemistry
PubMed ID3026452
Grant ListGM-27103 / GM / NIGMS NIH HHS / United States
GM-36327 / GM / NIGMS NIH HHS / United States

Weill Cornell Medicine Microbiology and Immunology 1300 York Avenue, Box 62 New York, NY 10065 Phone: (212) 746-6505 Fax: (212) 746-8587