Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres*
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F12%3A00057815" target="_blank" >RIV/00216224:14740/12:00057815 - isvavai.cz</a>
Result on the web
<a href="http://www.ncbi.nlm.nih.gov/pubmed/22815473" target="_blank" >http://www.ncbi.nlm.nih.gov/pubmed/22815473</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.M112.385591" target="_blank" >10.1074/jbc.M112.385591</a>
Alternative languages
Result language
angličtina
Original language name
Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres*
Original language description
Double-stranded regions of the telomeres are recognized by proteins containing Myb-like domains conferring specificity toward telomeric repeats. Although biochemical and structural studies revealed basic molecular principles involved in DNA binding, relatively little is known about evolutionary pathways leading to various types of Myb domain-containing proteins in divergent species of eukaryotes. Recently we identified a novel type of telomere-binding protein YlTay1p from the yeast Yarrowia lipolytica containing two Myb domains (Myb1, Myb2) very similar to the Myb domain of mammalian TRF1 and TRF2. In this study we prepared mutant versions of YlTay1p lacking Myb1, Myb2, or both Myb domains and found that YlTay1p carrying either Myb domain exhibits preferential affinity to both Y. lipolytica (GGGTTAGTCA)n and human (TTAGGG)n telomeric sequences.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
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)
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
The Journal of Biological Chemistry
ISSN
0021-9258
e-ISSN
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Volume of the periodical
287
Issue of the periodical within the volume
38
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
32206-32215
UT code for WoS article
000309059400057
EID of the result in the Scopus database
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