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

Result code in 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>

Alternative codes found

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

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10600 - Biological sciences

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

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

Publication year

2017

Confidentiality

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

Name of the periodical

Protoplasma

ISSN

0033-183X

e-ISSN

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Volume of the periodical

254

Issue of the periodical within the volume

4

Country of publishing house

AT - AUSTRIA

Number of pages

16

Pages from-to

1547-1562

UT code for WoS article

000403774000009

EID of the result in the Scopus database

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