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

J 2017

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

MAJERSKÁ, Jana, Petra PROCHÁZKOVÁ SCHRUMPFOVÁ, Ladislav DOKLADAL, Šárka SCHOŘOVÁ, Karel STEJSKAL et. al.

Základní údaje

Originální název

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

Autoři

MAJERSKÁ, Jana (703 Slovensko, domácí), Petra PROCHÁZKOVÁ SCHRUMPFOVÁ (203 Česká republika, domácí), Ladislav DOKLADAL (203 Česká republika), Šárka SCHOŘOVÁ (203 Česká republika, garant, domácí), Karel STEJSKAL (203 Česká republika, domácí), Michal OBOŘIL (203 Česká republika, domácí), David HONYS (203 Česká republika), Lucie KOZÁKOVÁ (203 Česká republika, domácí), Pavla SOVÁKOVÁ (203 Česká republika, domácí) a Eva SYKOROVA (203 Česká republika)

Vydání

Protoplasma, Wien, Springer-Verlag, 2017, 0033-183X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Rakousko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.457

Kód RIV

RIV/00216224:14740/17:00094874

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1007/s00709-016-1042-3

UT WoS

000403774000009

Klíčová slova anglicky

Telomerase; TAP-MS; AtPOT1a; Pontin; Reptin; PUR alpha 1

Štítky

CF PROT, rivok

Změněno: 26. 4. 2018 12:48, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

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.

Návaznosti

GA13-06943S, projekt VaV

Název: Strukturní a funkční komponenty rostlinných telomer

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

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

MUNI/C/0981/2010, interní kód MU

Název: Funkční charakterizace domén rostlinné telomerázy (Akronym: TAPTERT)

Investor: Masarykova univerzita, Funkční charakterizace domén rostlinné telomerázy, DO R. 2020 - Program rektora

Citovat

MAJERSKÁ, Jana, Petra PROCHÁZKOVÁ SCHRUMPFOVÁ, Ladislav DOKLADAL, Šárka SCHOŘOVÁ, Karel STEJSKAL, Michal OBOŘIL, David HONYS, Lucie KOZÁKOVÁ, Pavla SOVÁKOVÁ a Eva SYKOROVA. Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo. Protoplasma. Wien: Springer-Verlag, 2017, roč. 254, č. 4, s. 1547-1562. ISSN 0033-183X. Dostupné z: https://dx.doi.org/10.1007/s00709-016-1042-3.

@article{1386747,
   author = {Majerská, Jana and Procházková Schrumpfová, Petra and Dokladal, Ladislav and Schořová, Šárka and Stejskal, Karel and Obořil, Michal and Honys, David and Kozáková, Lucie and Sováková, Pavla and Sykorova, Eva},
   article_location = {Wien},
   article_number = {4},
   doi = {http://dx.doi.org/10.1007/s00709-016-1042-3},
   keywords = {Telomerase; TAP-MS; AtPOT1a; Pontin; Reptin; PUR alpha 1},
   language = {eng},
   issn = {0033-183X},
   journal = {Protoplasma},
   title = {Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo},
   url = {https://link.springer.com/article/10.1007%2Fs00709-016-1042-3},
   volume = {254},
   year = {2017}
}

TY  - JOUR
ID  - 1386747
AU  - Majerská, Jana - Procházková Schrumpfová, Petra - Dokladal, Ladislav - Schořová, Šárka - Stejskal, Karel - Obořil, Michal - Honys, David - Kozáková, Lucie - Sováková, Pavla - Sykorova, Eva
PY  - 2017
TI  - Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo
JF  - Protoplasma
VL  - 254
IS  - 4
SP  - 1547-1562
EP  - 1547-1562
PB  - Springer-Verlag
SN  - 0033183X
KW  - Telomerase
KW  - TAP-MS
KW  - AtPOT1a
KW  - Pontin
KW  - Reptin
KW  - PUR alpha 1
UR  - https://link.springer.com/article/10.1007%2Fs00709-016-1042-3
L2  - https://link.springer.com/article/10.1007%2Fs00709-016-1042-3
N2  - 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.
ER  -

MAJERSKÁ, Jana, Petra PROCHÁZKOVÁ SCHRUMPFOVÁ, Ladislav DOKLADAL, Šárka SCHOŘOVÁ, Karel STEJSKAL, Michal OBOŘIL, David HONYS, Lucie KOZÁKOVÁ, Pavla SOVÁKOVÁ a Eva SYKOROVA. Tandem affinity purification of AtTERT reveals putative interaction partners of plant telomerase in vivo. \textit{Protoplasma}. Wien: Springer-Verlag, 2017, roč.~254, č.~4, s.~1547-1562. ISSN~0033-183X. Dostupné z: https://dx.doi.org/10.1007/s00709-016-1042-3.

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