Telomere repeat binding proteins are functional components of
Arabidopsis telomeres and interact with telomerase

J 2014

Telomere repeat binding proteins are functional components of Arabidopsis telomeres and interact with telomerase

PROCHÁZKOVÁ SCHRUMPFOVÁ, Petra; Ivona VYCHODILOVÁ; Martina DVOŘÁČKOVÁ; Jana MAJERSKÁ; Ladislav DOKLÁDAL et al.

Základní údaje

Originální název

Telomere repeat binding proteins are functional components of Arabidopsis telomeres and interact with telomerase

Autoři

PROCHÁZKOVÁ SCHRUMPFOVÁ, Petra ; Ivona VYCHODILOVÁ; Martina DVOŘÁČKOVÁ ; Jana MAJERSKÁ; Ladislav DOKLÁDAL; Šárka SCHOŘOVÁ a Jiří FAJKUS

Vydání

The Plant Journal, Hoboken (USA), Blackwell Science, 2014, 0960-7412

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

Genetika a molekulární biologie

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 5.972

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/14:00073912

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

telomere protein interaction; telomere repeat binding (TRB); telomere; Arabidopsis thaliana; plant shelterin; telomerase

Štítky

kontrola MP, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 11. 3. 2015 10:56, Martina Prášilová

Anotace

V originále

Although telomere-binding proteins constitute an essential part of telomeres, in vivo data indicating the existence of a structure similar to mammalian shelterin complex in plants are limited. Partial characterization of a number of candidate proteins has not identified true components of plant shelterin or elucidated their functional mechanisms. Telomere repeat binding (TRB) proteins from Arabidopsis thaliana bind plant telomeric repeats through a Myb domain of the telobox type in vitro, and have been shown to interact with POT1b (Protection of telomeres 1). Here we demonstrate co-localization of TRB1 protein with telomeres in situ using fluorescence microscopy, as well as in vivo interaction using chromatin immunoprecipitation. Classification of the TRB1 protein as a component of plant telomeres is further confirmed by the observation of shortening of telomeres in knockout mutants of the trb1 gene. Moreover, TRB proteins physically interact with plant telomerase catalytic subunits. These findings integrate TRB proteins into the telomeric interactome of A. thaliana.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

EE2.3.30.0009, projekt VaV

Název: Zaměstnáním čerstvých absolventů doktorského studia k vědecké excelenci

GA13-06943S, projekt VaV

Název: Strukturní a funkční komponenty rostlinných telomer

Investor: Grantová agentura ČR, Strukturní a funkční komponenty rostlinných telomer

Citovat

PROCHÁZKOVÁ SCHRUMPFOVÁ, Petra; Ivona VYCHODILOVÁ; Martina DVOŘÁČKOVÁ; Jana MAJERSKÁ; Ladislav DOKLÁDAL; Šárka SCHOŘOVÁ a Jiří FAJKUS. Telomere repeat binding proteins are functional components of Arabidopsis telomeres and interact with telomerase. The Plant Journal. Hoboken (USA): Blackwell Science, 2014, roč. 77, č. 5, s. 770-781. ISSN 0960-7412. Dostupné z: https://doi.org/10.1111/tpj.12428.

@article{1199821,
   author = {Procházková Schrumpfová, Petra and Vychodilová, Ivona and Dvořáčková, Martina and Majerská, Jana and Dokládal, Ladislav and Schořová, Šárka and Fajkus, Jiří},
   article_location = {Hoboken (USA)},
   article_number = {5},
   doi = {https://doi.org/10.1111/tpj.12428},
   keywords = {telomere protein interaction; telomere repeat binding (TRB); telomere; Arabidopsis thaliana; plant shelterin; telomerase},
   language = {eng},
   issn = {0960-7412},
   journal = {The Plant Journal},
   title = {Telomere repeat binding proteins are functional components of Arabidopsis telomeres and interact with telomerase},
   url = {http://onlinelibrary.wiley.com/doi/10.1111/tpj.12428/epdf},
   volume = {77},
   year = {2014}
}

TY  - JOUR
ID  - 1199821
AU  - Procházková Schrumpfová, Petra - Vychodilová, Ivona - Dvořáčková, Martina - Majerská, Jana - Dokládal, Ladislav - Schořová, Šárka - Fajkus, Jiří
PY  - 2014
TI  - Telomere repeat binding proteins are functional components of Arabidopsis telomeres and interact with telomerase
JF  - The Plant Journal
VL  - 77
IS  - 5
SP  - 770-781
EP  - 770-781
PB  - Blackwell Science
SN  - 09607412
KW  - telomere protein interaction
KW  - telomere repeat binding (TRB)
KW  - telomere
KW  - Arabidopsis thaliana
KW  - plant shelterin
KW  - telomerase
UR  - http://onlinelibrary.wiley.com/doi/10.1111/tpj.12428/epdf
L2  - http://onlinelibrary.wiley.com/doi/10.1111/tpj.12428/epdf
N2  - Although telomere-binding proteins constitute an essential part of telomeres, in vivo data indicating the existence of a structure similar to mammalian shelterin complex in plants are limited. Partial characterization of a number of candidate proteins has not identified true components of plant shelterin or elucidated their functional mechanisms. Telomere repeat binding (TRB) proteins from Arabidopsis thaliana bind plant telomeric repeats through a Myb domain of the telobox type in vitro, and have been shown to interact with POT1b (Protection of telomeres 1). Here we demonstrate co-localization of TRB1 protein with telomeres in situ using fluorescence microscopy, as well as in vivo interaction using chromatin immunoprecipitation. Classification of the TRB1 protein as a component of plant telomeres is further confirmed by the observation of shortening of telomeres in knockout mutants of the trb1 gene. Moreover, TRB proteins physically interact with plant telomerase catalytic subunits. These findings integrate TRB proteins into the telomeric interactome of A. thaliana.
ER  -

PROCHÁZKOVÁ SCHRUMPFOVÁ, Petra; Ivona VYCHODILOVÁ; Martina DVOŘÁČKOVÁ; Jana MAJERSKÁ; Ladislav DOKLÁDAL; Šárka SCHOŘOVÁ a Jiří FAJKUS. Telomere repeat binding proteins are functional components of Arabidopsis telomeres and interact with telomerase. \textit{The Plant Journal}. Hoboken (USA): Blackwell Science, 2014, roč.~77, č.~5, s.~770-781. ISSN~0960-7412. Dostupné z: https://doi.org/10.1111/tpj.12428.

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