Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative study of telomere-binding specificity and kinetics
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F09%3A00323280" target="_blank" >RIV/68081707:_____/09:00323280 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative study of telomere-binding specificity and kinetics
Original language 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.
Czech name
Proteiny SMH z Arabidopsis thaliana: kvantitativní studie telomer-vazebné specifity a kinetiky
Czech description
Provedli jsme první kvantitativní studii vazby specificky rostlinných SMH proteinů k DNA. Interakce celých proteinů AtTRB1 a AtTRB3 s telomerovou DNA byly pro zjištění jejich vazebné stechiometrie a kinetidy analyzovány pomocí posunu v elektroforetické mobilitě, anizotropie fluorescence a povrchové plazmonové rezonance. Na základě těchto údajů představujeme model vazebné stechiometrie a uspořádání proteinů na telomerové DNA.
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2009
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biochemical Journal
ISSN
0264-6021
e-ISSN
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Volume of the periodical
419
Issue of the periodical within the volume
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Country of publishing house
GB - UNITED KINGDOM
Number of pages
8
Pages from-to
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UT code for WoS article
000264642800024
EID of the result in the Scopus database
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