An armadillo-domain protein participates in a telomerase interaction network

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F18%3A00101550" target="_blank" >RIV/00216224:14310/18:00101550 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081707:_____/18:00502448 RIV/61389030:_____/18:00502448

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s11103-018-0747-4" target="_blank" >http://dx.doi.org/10.1007/s11103-018-0747-4</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11103-018-0747-4" target="_blank" >10.1007/s11103-018-0747-4</a>

Jazyk výsledku

angličtina

Název v původním jazyce

An armadillo-domain protein participates in a telomerase interaction network

Popis výsledku v původním jazyce

The ARM protein interacts with both the N- and C-terminal domains of AtTERT in different cellular compartments. ARM interacts with CHR19 and TRF-like I family proteins that also bind AtTERT directly or through interaction with POT1a. The putative human ARM homolog co-precipitates telomerase activity and interacts with hTRF2 protein in vitro. Analysis of Arabidopsis arm mutants shows no obvious changes in telomere length or telomerase activity, suggesting that ARM is not essential for telomere maintenance. The observed interactions with telomerase and Myb-like domain proteins (TRF-like family I) may therefore reflect possible non-telomeric functions. Transcript levels of several DNA repair and ribosomal genes are affected in arm mutants, and ARM, likely in association with other proteins, suppressed expression of XRCC3 and RPSAA promoter constructs in luciferase reporter assays. In conclusion, ARM can participate in non-telomeric functions of telomerase, and can also perform its own telomerase-independent functions.

Název v anglickém jazyce

An armadillo-domain protein participates in a telomerase interaction network

Popis výsledku anglicky

The ARM protein interacts with both the N- and C-terminal domains of AtTERT in different cellular compartments. ARM interacts with CHR19 and TRF-like I family proteins that also bind AtTERT directly or through interaction with POT1a. The putative human ARM homolog co-precipitates telomerase activity and interacts with hTRF2 protein in vitro. Analysis of Arabidopsis arm mutants shows no obvious changes in telomere length or telomerase activity, suggesting that ARM is not essential for telomere maintenance. The observed interactions with telomerase and Myb-like domain proteins (TRF-like family I) may therefore reflect possible non-telomeric functions. Transcript levels of several DNA repair and ribosomal genes are affected in arm mutants, and ARM, likely in association with other proteins, suppressed expression of XRCC3 and RPSAA promoter constructs in luciferase reporter assays. In conclusion, ARM can participate in non-telomeric functions of telomerase, and can also perform its own telomerase-independent functions.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

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OECD FORD obor

10611 - Plant sciences, botany

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2018

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Plant Molecular Biology

ISSN

0167-4412

e-ISSN

—

Svazek periodika

97

Číslo periodika v rámci svazku

4-5

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

14

Strana od-do

407-420

Kód UT WoS článku

000438981700009

EID výsledku v databázi Scopus

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