Synergism of the Two Myb Domains of Tay1 Protein Results in
High Affinity Binding to Telomeres*

J 2012

Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres*

VISACKA, Katarina; Ctirad HOFR; Smaranda WILLCOX; Ivona NEČASOVÁ; Jana PAVLOUŠKOVÁ et al.

Základní údaje

Originální název

Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres*

Autoři

Vydání

The Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 2012, 0021-9258

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.651

Kód RIV

RIV/00216224:14740/12:00057815

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1074/jbc.M112.385591

UT WoS

000309059400057

Klíčová slova anglicky

DNA-BINDING; ARABIDOPSIS-THALIANA; COMPLEX; TRF1; IDENTIFICATION; RECOGNITION; SPECIFICITY; PROTECTION; EVOLUTION; GENOME

Štítky

ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 18. 1. 2017 09:07, prof. RNDr. Jiří Fajkus, CSc.

Anotace

V originále

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.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GAP205/12/0550, projekt VaV

Název: Dynamika vzniku shelterinového komplexu

Investor: Grantová agentura ČR, Dynamika vzniku shelterinového komplexu

Přiložené soubory

2012_JBC_Visacka.pdf

Požádat o autorskou verzi souboru

Citovat

VISACKA, Katarina; Ctirad HOFR; Smaranda WILLCOX; Ivona NEČASOVÁ; Jana PAVLOUŠKOVÁ; Regina SEPSIOVA; Michaela WIMMEROVÁ; Lucia SIMONICOVA; Jozef NOSEK; Jiří FAJKUS; Jack D. GRIFFITH a Lubomir TOMASKA. Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres*. The Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2012, roč. 287, č. 38, s. 32206-32215. ISSN 0021-9258. Dostupné z: https://doi.org/10.1074/jbc.M112.385591.

@article{1073536,
   author = {Visacka, Katarina and Hofr, Ctirad and Willcox, Smaranda and Nečasová, Ivona and Pavloušková, Jana and Sepsiova, Regina and Wimmerová, Michaela and Simonicova, Lucia and Nosek, Jozef and Fajkus, Jiří and Griffith, Jack D. and Tomaska, Lubomir},
   article_location = {Bethesda, USA},
   article_number = {38},
   doi = {https://doi.org/10.1074/jbc.M112.385591},
   keywords = {DNA-BINDING; ARABIDOPSIS-THALIANA; COMPLEX; TRF1; IDENTIFICATION; RECOGNITION; SPECIFICITY; PROTECTION; EVOLUTION; GENOME},
   language = {eng},
   issn = {0021-9258},
   journal = {The Journal of Biological Chemistry},
   title = {Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres*},
   url = {http://www.ncbi.nlm.nih.gov/pubmed/22815473},
   volume = {287},
   year = {2012}
}

TY  - JOUR
ID  - 1073536
AU  - Visacka, Katarina - Hofr, Ctirad - Willcox, Smaranda - Nečasová, Ivona - Pavloušková, Jana - Sepsiova, Regina - Wimmerová, Michaela - Simonicova, Lucia - Nosek, Jozef - Fajkus, Jiří - Griffith, Jack D. - Tomaska, Lubomir
PY  - 2012
TI  - Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres*
JF  - The Journal of Biological Chemistry
VL  - 287
IS  - 38
SP  - 32206-32215
EP  - 32206-32215
PB  - Amer. Soc. Biochem. Mol. Biol.
SN  - 00219258
KW  - DNA-BINDING
KW  - ARABIDOPSIS-THALIANA
KW  - COMPLEX
KW  - TRF1
KW  - IDENTIFICATION
KW  - RECOGNITION
KW  - SPECIFICITY
KW  - PROTECTION
KW  - EVOLUTION
KW  - GENOME
UR  - http://www.ncbi.nlm.nih.gov/pubmed/22815473
L2  - http://www.ncbi.nlm.nih.gov/pubmed/22815473
N2  - 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.
ER  -

VISACKA, Katarina; Ctirad HOFR; Smaranda WILLCOX; Ivona NEČASOVÁ; Jana PAVLOUŠKOVÁ; Regina SEPSIOVA; Michaela WIMMEROVÁ; Lucia SIMONICOVA; Jozef NOSEK; Jiří FAJKUS; Jack D. GRIFFITH a Lubomir TOMASKA. Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres*. \textit{The Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2012, roč.~287, č.~38, s.~32206-32215. ISSN~0021-9258. Dostupné z: https://doi.org/10.1074/jbc.M112.385591.

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