Detailed Information on Publication Record
2009
Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative study of telomere-binding specifity and kinetics
HOFR, Ctirad, Pavla ŠULTESOVÁ, Michal ZIMMERMANN, Iva MOZGOVÁ, Petra PROCHÁZKOVÁ SCHRUMPFOVÁ et. al.Basic information
Original name
Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative study of telomere-binding specifity and kinetics
Name in Czech
Proteiny SMH z Arabidopsis thaliana: kvantitativní studie telomer-vazebné specifity a kinetiky
Authors
HOFR, Ctirad (203 Czech Republic, guarantor, belonging to the institution), Pavla ŠULTESOVÁ (203 Czech Republic, belonging to the institution), Michal ZIMMERMANN (203 Czech Republic, belonging to the institution), Iva MOZGOVÁ (203 Czech Republic, belonging to the institution), Petra PROCHÁZKOVÁ SCHRUMPFOVÁ (203 Czech Republic, belonging to the institution), Michaela WIMMEROVÁ (203 Czech Republic, belonging to the institution) and Jiří FAJKUS (203 Czech Republic, belonging to the institution)
Edition
BIOCHEMICAL JOURNAL, ENGLAND, PORTLAND PRESS LTD, 2009, 0264-6021
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
Genetics and molecular biology
Country of publisher
United Kingdom of Great Britain and Northern Ireland
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 5.155
RIV identification code
RIV/00216224:14310/09:00028470
Organization unit
Faculty of Science
UT WoS
000264642800024
Keywords in English
Fluorescence anisotropy; single-Myb-histone protein (SMH protein); surface plasmon resonance; telomere protein DNA interaction
Tags
Tags
International impact, Reviewed
Změněno: 13/1/2012 22:17, prof. RNDr. Jiří Fajkus, CSc.
V originále
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.
In Czech
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 kinetiky analyzovány pomocí posunu v elektroforetické mobilitě, anizotropie fluorescence a povrchové plazmonové rezonance. Nazákladě těchto údajů představujeme model vazebné stechiometrie a uspořádání proteinů na telomerové DNA.
Links
| MSM0021622415, plan (intention) |
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