Telomerase Interaction Partners–Insight from Plants
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...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/1/368 |
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| author | Jana Fulnečková Ladislav Dokládal Karolína Kolářová Martina Nešpor Dadejová Klára Procházková Sabina Gomelská Martin Sivčák Kateřina Adamusová Martin Lyčka Vratislav Peska Martina Dvořáčková Eva Sýkorová |
| author_facet | Jana Fulnečková Ladislav Dokládal Karolína Kolářová Martina Nešpor Dadejová Klára Procházková Sabina Gomelská Martin Sivčák Kateřina Adamusová Martin Lyčka Vratislav Peska Martina Dvořáčková Eva Sýkorová |
| author_sort | Jana Fulnečková |
| collection | DOAJ |
| description | 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 <i>Arabidopsis</i> 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. |
| first_indexed | 2024-03-10T03:38:15Z |
| format | Article |
| id | doaj.art-0dfa520d5342447685dfe73a5ba2f8c8 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T03:38:15Z |
| publishDate | 2021-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-0dfa520d5342447685dfe73a5ba2f8c82023-11-23T11:38:56ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-12-0123136810.3390/ijms23010368Telomerase Interaction Partners–Insight from PlantsJana Fulnečková0Ladislav Dokládal1Karolína Kolářová2Martina Nešpor Dadejová3Klára Procházková4Sabina Gomelská5Martin Sivčák6Kateřina Adamusová7Martin Lyčka8Vratislav Peska9Martina Dvořáčková10Eva Sýkorová11Department of Cell Biology and Radiobiology, Institute of Biophysics of the Czech Academy of Sciences, CZ-61265 Brno, Czech RepublicDepartment of Cell Biology and Radiobiology, Institute of Biophysics of the Czech Academy of Sciences, CZ-61265 Brno, Czech RepublicDepartment of Cell Biology and Radiobiology, Institute of Biophysics of the Czech Academy of Sciences, CZ-61265 Brno, Czech RepublicMendel Centre for Plant Genomics and Proteomics, Central European Institute of Technology, Masaryk University, CZ-62500 Brno, Czech RepublicDepartment of Cell Biology and Radiobiology, Institute of Biophysics of the Czech Academy of Sciences, CZ-61265 Brno, Czech RepublicDepartment of Cell Biology and Radiobiology, Institute of Biophysics of the Czech Academy of Sciences, CZ-61265 Brno, Czech RepublicDepartment of Cell Biology and Radiobiology, Institute of Biophysics of the Czech Academy of Sciences, CZ-61265 Brno, Czech RepublicDepartment of Cell Biology and Radiobiology, Institute of Biophysics of the Czech Academy of Sciences, CZ-61265 Brno, Czech RepublicNational Centre for Biomolecular Research, Faculty of Science, Masaryk University, CZ-61137 Brno, Czech RepublicDepartment of Cell Biology and Radiobiology, Institute of Biophysics of the Czech Academy of Sciences, CZ-61265 Brno, Czech RepublicMendel Centre for Plant Genomics and Proteomics, Central European Institute of Technology, Masaryk University, CZ-62500 Brno, Czech RepublicDepartment of Cell Biology and Radiobiology, Institute of Biophysics of the Czech Academy of Sciences, CZ-61265 Brno, Czech RepublicTelomerase, 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 <i>Arabidopsis</i> 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.https://www.mdpi.com/1422-0067/23/1/368protein–protein interactionreplicationmitochondriachromatintransportfolding |
| spellingShingle | Jana Fulnečková Ladislav Dokládal Karolína Kolářová Martina Nešpor Dadejová Klára Procházková Sabina Gomelská Martin Sivčák Kateřina Adamusová Martin Lyčka Vratislav Peska Martina Dvořáčková Eva Sýkorová Telomerase Interaction Partners–Insight from Plants International Journal of Molecular Sciences protein–protein interaction replication mitochondria chromatin transport folding |
| title | Telomerase Interaction Partners–Insight from Plants |
| title_full | Telomerase Interaction Partners–Insight from Plants |
| title_fullStr | Telomerase Interaction Partners–Insight from Plants |
| title_full_unstemmed | Telomerase Interaction Partners–Insight from Plants |
| title_short | Telomerase Interaction Partners–Insight from Plants |
| title_sort | telomerase interaction partners insight from plants |
| topic | protein–protein interaction replication mitochondria chromatin transport folding |
| url | https://www.mdpi.com/1422-0067/23/1/368 |
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