Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F17%3A00094874" target="_blank" >RIV/00216224:14740/17:00094874 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081707:_____/17:00492527 RIV/61389030:_____/17:00492527

Výsledek na webu

<a href="https://link.springer.com/article/10.1007%2Fs00709-016-1042-3" target="_blank" >https://link.springer.com/article/10.1007%2Fs00709-016-1042-3</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00709-016-1042-3" target="_blank" >10.1007/s00709-016-1042-3</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo

Popis výsledku v původním jazyce

The life cycle of telomerase involves dynamic and complex interactions between proteins within multiple macromolecular networks. Elucidation of these associations is a key to understanding the regulation of telomerase under diverse physiological and pathological conditions from telomerase biogenesis, through telomere recruitment and elongation, to its non-canonical activities outside of telomeres. We used tandem affinity purification coupled to mass spectrometry to build an interactome of the telomerase catalytic subunit AtTERT, using Arabidopsis thaliana suspension cultures. We then examined interactions occurring at the AtTERT N-terminus, which is thought to fold into a discrete domain connected to the rest of the molecule via a flexible linker. Bioinformatic analyses revealed that interaction partners of AtTERT have a range of molecular functions, a subset of which is specific to the network around its N-terminus. A significant number of proteins co-purifying with the N-terminal constructs have been implicated in cell cycle and developmental processes, as would be expected of bona fide regulatory interactions and we have confirmed experimentally the direct nature of selected interactions. To examine AtTERT protein-protein interactions from another perspective, we also analysed AtTERT interdomain contacts to test potential dimerization of AtTERT. In total, our results provide an insight into the composition and architecture of the plant telomerase complex and this will aid in delineating molecular mechanisms of telomerase functions.

Název v anglickém jazyce

Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo

Popis výsledku anglicky

The life cycle of telomerase involves dynamic and complex interactions between proteins within multiple macromolecular networks. Elucidation of these associations is a key to understanding the regulation of telomerase under diverse physiological and pathological conditions from telomerase biogenesis, through telomere recruitment and elongation, to its non-canonical activities outside of telomeres. We used tandem affinity purification coupled to mass spectrometry to build an interactome of the telomerase catalytic subunit AtTERT, using Arabidopsis thaliana suspension cultures. We then examined interactions occurring at the AtTERT N-terminus, which is thought to fold into a discrete domain connected to the rest of the molecule via a flexible linker. Bioinformatic analyses revealed that interaction partners of AtTERT have a range of molecular functions, a subset of which is specific to the network around its N-terminus. A significant number of proteins co-purifying with the N-terminal constructs have been implicated in cell cycle and developmental processes, as would be expected of bona fide regulatory interactions and we have confirmed experimentally the direct nature of selected interactions. To examine AtTERT protein-protein interactions from another perspective, we also analysed AtTERT interdomain contacts to test potential dimerization of AtTERT. In total, our results provide an insight into the composition and architecture of the plant telomerase complex and this will aid in delineating molecular mechanisms of telomerase functions.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10600 - Biological sciences

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

2017

Kód důvěrnosti údajů

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

Název periodika

Protoplasma

ISSN

0033-183X

e-ISSN

—

Svazek periodika

254

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

AT - Rakouská republika

Počet stran výsledku

16

Strana od-do

1547-1562

Kód UT WoS článku

000403774000009

EID výsledku v databázi Scopus

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