Telomerase Interaction Partners-Insight from Plants

0553787 - BFÚ 2023 RIV CH eng J - Článek v odborném periodiku
Fulnečková, Jana - Dokládal, Ladislav - Kolářová, Karolína - Nespor Dadejova, M. - Procházková, K. - Gomelska, Sabina - Sivčák, Martin - Adamusová, Kateřina - Lycka, M. - Peška, Vratislav - Dvořáčková, M. - Sýkorová, Eva
Telomerase Interaction Partners-Insight from Plants.
International Journal of Molecular Sciences. Roč. 23, č. 1 (2022), č. článku 368. E-ISSN 1422-0067
Grant CEP: GA ČR(CZ) GA18-07027S; GA MŠMT EF15_003/0000477
Institucionální podpora: RVO:68081707
Klíčová slova: somatic homologous recombination * maintenance complex mcm * histone chaperones * embryo development * distinct roles * end-protection
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 5.6, rok: 2022
Způsob publikování: Open access
https://www.mdpi.com/1422-0067/23/1/368

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.
Trvalý link: https://hdl.handle.net/11104/0340280