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

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...

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Veröffentlicht in:	Biochemistry (Easton) 1986-11, Vol.25 (23), p.7362-7368
Hauptverfasser:	Brougham, Michael J, Rowe, Thomas C, Holloman, William K
Format:	Artikel
Sprache:	eng
Schlagworte:	ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE ADN Analytical, structural and metabolic biochemistry Basidiomycota - enzymology Binding Sites Biological and medical sciences DNA DNA topoisomerase DNA Topoisomerases, Type I - metabolism DNA, Single-Stranded - metabolism Enzymes and enzyme inhibitors ENZYMIC ACTIVITY Fundamental and applied biological sciences. Psychology Isomerases Kinetics phosphodiesters Protein Binding RECOMBINACION RECOMBINAISON RECOMBINATION Substrate Specificity TIROSINA TYROSINE USTILAGO Ustilago - enzymology
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