Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative study of telomere-binding specificity and kinetics
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
19102728
DOI
10.1042/bj20082195
PII: BJ20082195
Knihovny.cz E-resources
- MeSH
- Arabidopsis genetics metabolism MeSH
- Models, Biological MeSH
- Fluorescence Polarization MeSH
- Histones genetics metabolism MeSH
- Kinetics MeSH
- Surface Plasmon Resonance MeSH
- Arabidopsis Proteins genetics metabolism MeSH
- Electrophoretic Mobility Shift Assay MeSH
- Telomere genetics metabolism MeSH
- Protein Binding genetics MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Histones MeSH
- Arabidopsis Proteins MeSH
Proteins that bind telomeric DNA modulate the structure of chromosome ends and control telomere function and maintenance. It has been shown that AtTRB (Arabidopsis thaliana telomere-repeat-binding factor) proteins from the SMH (single-Myb-histone) family selectively bind double-stranded telomeric DNA and interact with the telomeric protein AtPOT1b (A. thaliana protection of telomeres 1b), which is involved in telomere capping. In the present study, we performed the first quantitative DNA-binding study of this plant-specific family of 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. Kinetic analyses at different salt conditions enabled us to estimate the electrostatic component of binding and explain different affinities of the two proteins to telomeric DNA. On the basis of available data, a putative model explaining the binding stoichiometry and the protein arrangement on telomeric DNA is presented.
References provided by Crossref.org
Origin, Diversity, and Evolution of Telomere Sequences in Plants
Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it
Telomere- and Telomerase-Associated Proteins and Their Functions in the Plant Cell
Telomere binding protein TRB1 is associated with promoters of translation machinery genes in vivo
Human Rap1 modulates TRF2 attraction to telomeric DNA
