Detailed Information on Publication Record
2024
Characterisation of the Arabidopsis thaliana telomerase TERT-TR complex
ŠTEFANOVIE, Barbora, Leon Paul JENNER, Lucie BOZDĚCHOVÁ, Petr FAJKUS, Eva SÝKOROVÁ et. al.Basic information
Original name
Characterisation of the Arabidopsis thaliana telomerase TERT-TR complex
Authors
ŠTEFANOVIE, Barbora (703 Slovakia, belonging to the institution), Leon Paul JENNER (826 United Kingdom of Great Britain and Northern Ireland), Lucie BOZDĚCHOVÁ (203 Czech Republic, belonging to the institution), Petr FAJKUS (203 Czech Republic, belonging to the institution), Eva SÝKOROVÁ (203 Czech Republic), Jiří FAJKUS (203 Czech Republic, belonging to the institution) and Jan PALEČEK (203 Czech Republic, guarantor, belonging to the institution)
Edition
Plant Molecular Biology, Dordrecht (Netherlands), Springer, 2024, 0167-4412
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10608 Biochemistry and molecular biology
Country of publisher
Netherlands
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 5.100 in 2022
Organization unit
Faculty of Science
UT WoS
001222709400002
Keywords (in Czech)
A.thaliana telomerasa; AtTERT; AtTR; Protein-RNA interakce; kvasinkový troj-hybridní systém
Keywords in English
A.thaliana telomerase; AtTERT; AtTR; Protein-RNA interactions; Yeast three-hybrid
Tags
International impact, Reviewed
Změněno: 7/8/2024 13:49, prof. RNDr. Jiří Fajkus, CSc.
Abstract
V originále
Most eukaryotic organisms employ a telomerase complex for the maintenance of chromosome ends. The core of this complex is composed of telomerase reverse transcriptase (TERT) and telomerase RNA (TR) subunits. The TERT reverse transcriptase (RT) domain synthesises telomeric DNA using the TR template sequence. The other TERT domains contribute to this process in different ways. In particular, the TERT RNA-binding domain (TRBD) interacts with specific TR motif(s). Using a yeast 3-hybrid system, we show the critical role of Arabidopsis thaliana (At) TRBD and embryophyta-conserved KRxR motif in the unstructured linker preceding the TRBD domain for binding to the recently identified AtTR subunit. We also show the essential role of the predicted P4 stem and pseudoknot AtTR structures and provide evidence for the binding of AtTRBD to pseudoknot and KRxR motif stabilising interaction with the P4 stem structure. Our results thus provide the first insight into the core part of the plant telomerase complex.
Links
EH22_008/0004581, research and development project |
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GX20-01331X, research and development project |
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MUNI/R/1142/2021, interní kód MU |
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