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

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Authors	HOFR Ctirad ŠULTESOVÁ Pavla ZIMMERMANN Michal MOZGOVÁ Iva PROCHÁZKOVÁ SCHRUMPFOVÁ Petra WIMMEROVÁ Michaela FAJKUS Jiří
Year of publication	2009
Type	Article in Periodical
Magazine / Source	BIOCHEMICAL JOURNAL
MU Faculty or unit	Faculty of Science
Citation
Field	Genetics and molecular biology
Keywords	Fluorescence anisotropy; single-Myb-histone protein (SMH protein); surface plasmon resonance; telomere protein DNA interaction
Description	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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