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@article{2215599,
author = {Fulnečková, Jana and Dokládal, Ladislav and Kolářová, Karolína and Nešpor Dadejová, Martina and Prochazkova, Klara and Gomelská, Sabina and Sivčák, Martin and Adamusová, Kateřina and Lyčka, Martin and Peška, Vratislav and Dvořáčková, Martina and Sýkorová, Eva},
article_location = {Basel},
article_number = {1},
doi = {http://dx.doi.org/10.3390/ijms23010368},
keywords = {protein-protein interaction; replication; mitochondria; chromatin; transport; folding; telomerase; Arabidopsis},
language = {eng},
issn = {1422-0067},
journal = {International Journal of Molecular Sciences},
title = {Telomerase Interaction Partners-Insight from Plants},
url = {https://doi.org/10.3390/ijms23010368},
volume = {23},
year = {2022}
}
TY - JOUR
ID - 2215599
AU - Fulnečková, Jana - Dokládal, Ladislav - Kolářová, Karolína - Nešpor Dadejová, Martina - Prochazkova, Klara - Gomelská, Sabina - Sivčák, Martin - Adamusová, Kateřina - Lyčka, Martin - Peška, Vratislav - Dvořáčková, Martina - Sýkorová, Eva
PY - 2022
TI - Telomerase Interaction Partners-Insight from Plants
JF - International Journal of Molecular Sciences
VL - 23
IS - 1
SP - 368
EP - 368
PB - Multidisciplinary Digital Publishing Institute
SN - 14220067
KW - protein-protein interaction
KW - replication
KW - mitochondria
KW - chromatin
KW - transport
KW - folding
KW - telomerase
KW - Arabidopsis
UR - https://doi.org/10.3390/ijms23010368
N2 - Telomerase, an essential enzyme that maintains chromosome ends, is important for genome integrity and organism development. Various hypotheses have been proposed in human, ciliate and yeast systems to explain the coordination of telomerase holoenzyme assembly and the timing of telomerase performance at telomeres during DNA replication or repair. However, a general model is still unclear, especially pathways connecting telomerase with proposed non-telomeric functions. To strengthen our understanding of telomerase function during its intracellular life, we report on interactions of several groups of proteins with the Arabidopsis telomerase protein subunit (AtTERT) and/or a component of telomerase holoenzyme, POT1a protein. Among these are the nucleosome assembly proteins (NAP) and the minichromosome maintenance (MCM) system, which reveal new insights into the telomerase interaction network with links to telomere chromatin assembly and replication. A targeted investigation of 176 candidate proteins demonstrated numerous interactions with nucleolar, transport and ribosomal proteins, as well as molecular chaperones, shedding light on interactions during telomerase biogenesis. We further identified protein domains responsible for binding and analyzed the subcellular localization of these interactions. Moreover, additional interaction networks of NAP proteins and the DOMINO1 protein were identified. Our data support an image of functional telomerase contacts with multiprotein complexes including chromatin remodeling and cell differentiation pathways.
ER -
FULNEČKOVÁ, Jana, Ladislav DOKLÁDAL, Karolína KOLÁŘOVÁ, Martina NEŠPOR DADEJOVÁ, Klara PROCHAZKOVA, Sabina GOMELSKÁ, Martin SIVČÁK, Kateřina ADAMUSOVÁ, Martin LYČKA, Vratislav PEŠKA, Martina DVOŘÁČKOVÁ and Eva SÝKOROVÁ. Telomerase Interaction Partners-Insight from Plants. \textit{International Journal of Molecular Sciences}. Basel: Multidisciplinary Digital Publishing Institute, 2022, vol.~23, No~1, p.~368-395. ISSN~1422-0067. Available from: https://dx.doi.org/10.3390/ijms23010368.
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