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Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative study of telomere-binding specifity and kinetics

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Original title:Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative study of telomere-binding specifity and kinetics
Authors:Ctirad Hofr, Pavla Šultesová, Michal Zimmermann, Iva Mozgová, Petra Procházková Schrumpfová, Michaela Wimmerová, Jiří Fajkus
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Original language:English
Field:Genetics and molecular biology
Type:Article in Periodical
Keywords:Fluorescence anisotropy; single-Myb-histone protein (SMH protein); surface plasmon resonance; telomere protein DNA interaction

We performed the first quantitative DNA-binding study of the plant-specific family of SMH proteins. Interactions of full-length proteins AtTRB1 and AtTRB3 with telomeric DNA were analysed by electrophoretic mobility-shift assay, fluorescence anisotropy and surface plasmon resonance to reveal their binding stoichiometry and kinetics. Based on these data, a model explaining the binding stoichiometry and the protein arrangement on telomeric DNA is presented.

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