Open Access
Journal of Biological Chemistry, volume 287, issue 38, pages 32206-32215
Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres
Visacka Katarina
1
,
Hofr Ctirad
2
,
Willcox Smaranda
3
,
Nečasová Ivona
2
,
Pavloušková Jana
2
,
Sepšiová Regina
1
,
Wimmerová Michaela
2
,
Simonicova Lucia
1
,
Nosek Jozef
1
,
Fajkus J.
2
,
Griffith Jack D.
3
,
Tomáška Ľubomír
1
1
Department of Genetics and Biochemistry, Comenius University, Faculty of Natural Sciences, Mlynska dolina, 842 15 Bratislava, Slovakia
|
2
Faculty of Science and Central European Institute of Technology, Masaryk University, Kamenice 5, Brno, CZ-62500, Czech Republic
|
3
¶Lineberger Comprehensive Cancer Center and Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, North Carolina 27599
|
Publication type: Journal Article
Publication date: 2012-09-01
Journal:
Journal of Biological Chemistry
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor: 4.8
ISSN: 00219258, 1083351X
PubMed ID:
22815473
Biochemistry
Molecular Biology
Cell Biology
Abstract
Background: In contrast to mammalian TRF1 and TRF2, yeast telomeric protein YlTay1 possesses two Myb domains. Results: Kinetic and thermodynamic analyses revealed binding properties of individual Myb domains of YlTay1p. Conclusion: The combined presence of the two Myb domains synergistically increases the affinity of YlTay1p to telomeric DNA. Significance: The study demonstrates evolutionary tinkering with telomere-associated proteins. 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. Quantitative measurements of the protein binding to telomeric DNA revealed that the presence of both Myb domains is required for a high affinity of YlTay1p to either telomeric repeat. Additionally, we performed detailed thermodynamic analysis of the YlTay1p interaction with its cognate telomeric DNA, which is to our knowledge the first energetic description of a full-length telomeric-protein binding to DNA. Interestingly, when compared with human TRF1 and TRF2 proteins, YlTay1p exhibited higher affinity not only for Y. lipolytica telomeres but also for human telomeric sequences. The duplication of the Myb domain region in YlTay1p thus produces a synergistic effect on its affinity toward the cognate telomeric sequence, alleviating the need for homodimerization observed in TRF-like proteins possessing a single Myb domain.
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- We do not take into account publications that without a DOI.
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Visacka K. et al. Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres // Journal of Biological Chemistry. 2012. Vol. 287. No. 38. pp. 32206-32215.
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Visacka K., Hofr C., Willcox S., Nečasová I., Pavloušková J., Sepšiová R., Wimmerová M., Simonicova L., Nosek J., Fajkus J., Griffith J., Tomáška Ľ. Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres // Journal of Biological Chemistry. 2012. Vol. 287. No. 38. pp. 32206-32215.
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TY - JOUR
DO - 10.1074/jbc.M112.385591
UR - https://doi.org/10.1074%2Fjbc.M112.385591
TI - Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres
T2 - Journal of Biological Chemistry
AU - Visacka, Katarina
AU - Hofr, Ctirad
AU - Willcox, Smaranda
AU - Nečasová, Ivona
AU - Pavloušková, Jana
AU - Sepšiová, Regina
AU - Wimmerová, Michaela
AU - Simonicova, Lucia
AU - Nosek, Jozef
AU - Fajkus, J.
AU - Griffith, Jack D.
AU - Tomáška, Ľubomír
PY - 2012
DA - 2012/09/01 00:00:00
PB - American Society for Biochemistry and Molecular Biology
SP - 32206-32215
IS - 38
VL - 287
PMID - 22815473
SN - 0021-9258
SN - 1083-351X
ER -
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@article{2012_Visacka,
author = {Katarina Visacka and Ctirad Hofr and Smaranda Willcox and Ivona Nečasová and Jana Pavloušková and Regina Sepšiová and Michaela Wimmerová and Lucia Simonicova and Jozef Nosek and J. Fajkus and Jack D. Griffith and Ľubomír Tomáška},
title = {Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres},
journal = {Journal of Biological Chemistry},
year = {2012},
volume = {287},
publisher = {American Society for Biochemistry and Molecular Biology},
month = {sep},
url = {https://doi.org/10.1074%2Fjbc.M112.385591},
number = {38},
pages = {32206--32215},
doi = {10.1074/jbc.M112.385591}
}
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Visacka, Katarina, et al. “Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres.” Journal of Biological Chemistry, vol. 287, no. 38, Sep. 2012, pp. 32206-32215. https://doi.org/10.1074%2Fjbc.M112.385591.