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DC Field | Value | Language |
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dc.contributor.author | Fulneček, Jaroslav | - |
dc.contributor.author | Klimentová, Eva | - |
dc.contributor.author | Cairo, Albert | - |
dc.contributor.author | Bukovcakova, Sona Valuchova | - |
dc.contributor.author | Alexiou, Panagiotis | - |
dc.contributor.author | Prokop, Zbynek | - |
dc.contributor.author | Riha, Karel | - |
dc.date.accessioned | 2024-01-12T09:47:11Z | - |
dc.date.available | 2024-01-12T09:47:11Z | - |
dc.date.issued | 2023 | - |
dc.identifier.citation | Fulneček, J., Klimentová, E., Cairo, A., Bukovcakova, S. V., Alexiou, P., Prokop, Z., & Riha, K. (2023). The SAP domain of Ku facilitates its efficient loading onto DNA ends. Nucleic Acids Research, 51(21), 11706-11716. | en_GB |
dc.identifier.uri | https://www.um.edu.mt/library/oar/handle/123456789/117167 | - |
dc.description.abstract | The evolutionarily conserved DNA repair complex Ku serves as the primary sensor of free DNA ends in eukaryotic cells. Its rapid association with DNA ends is crucial for several cellular processes, including non-homologous end joining (NHEJ) DNA repair and telomere protection. In this study, we conducted a transient kinetic analysis to investigate the impact of the SAP domain on individual phases of the Ku–DNA interaction. Specifically, we examined the initial binding, the subsequent docking of Ku onto DNA, and sliding of Ku along DNA. Our findings revealed that the C-terminal SAP domain of Ku70 facilitates the initial phases of the Ku–DNA interaction but does not affect the sliding process. This suggests that the SAP domain may either establish the first interactions with DNA, or stabilize these initial interactions during loading. To assess the biological role of the SAP domain, we generated Arabidopsis plants expressing Ku lacking the SAP domain. Intriguingly, despite the decreased efficiency of the ΔSAP Ku complex in loading onto DNA, the mutant plants exhibited full proficiency in classical NHEJ and telomere maintenance. This indicates that the speed with which Ku loads onto telomeres or DNA double-strand breaks is not the decisive factor in stabilizing these DNA structures. | en_GB |
dc.language.iso | en | en_GB |
dc.publisher | Oxford University Press | en_GB |
dc.rights | info:eu-repo/semantics/openAccess | en_GB |
dc.subject | DNA -- Analysis | en_GB |
dc.subject | Algorithms | en_GB |
dc.subject | Application software | en_GB |
dc.subject | Database management | en_GB |
dc.title | The SAP domain of Ku facilitates its efficient loading onto DNA ends | en_GB |
dc.type | article | en_GB |
dc.rights.holder | The copyright of this work belongs to the author(s)/publisher. The rights of this work are as defined by the appropriate Copyright Legislation or as modified by any successive legislation. Users may access this work and can make use of the information contained in accordance with the Copyright Legislation provided that the author must be properly acknowledged. Further distribution or reproduction in any format is prohibited without the prior permission of the copyright holder | en_GB |
dc.description.reviewed | peer-reviewed | en_GB |
dc.identifier.doi | 10.1093/nar/gkad850 | - |
dc.publication.title | Nucleic Acids Research | en_GB |
Appears in Collections: | Scholarly Works - FacHScABS |
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The_SAP_domain_of_Ku_facilitates_its_efficient_loading_onto_DNA_ends.pdf | 781.42 kB | Adobe PDF | View/Open |
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