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