HOFR, Ctirad, Pavla ŠULTESOVÁ, Michal ZIMMERMANN, Iva MOZGOVÁ, Petra PROCHÁZKOVÁ SCHRUMPFOVÁ, Michaela WIMMEROVÁ and Jiří FAJKUS. Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative study of telomere-binding specifity and kinetics. BIOCHEMICAL JOURNAL. ENGLAND: PORTLAND PRESS LTD, 2009, vol. 419, Neuveden, p. 221-228. ISSN 0264-6021.
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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
Original language English
Type of outcome Article in a journal
Field of Study Genetics and molecular biology
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
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 fluorescence anisotropy, single-Myb-histone protein (SMH protein), surface plasmon resonance, telomere protein DNA interaction
Tags International impact, Reviewed
Changed by Changed by: prof. RNDr. Jiří Fajkus, CSc., učo 28574. Changed: 13/1/2012 22:17.
Abstract
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.
Abstract (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)Name: Molekulární podstata buněčných a tkáňových regulací
Investor: Ministry of Education, Youth and Sports of the CR, Molecular basis of cell and tissue regulations
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