Biochemical characterization of the meiosis-essential yet evolutionarily divergent topoisomerase VIB-like protein MTOPVIB from Arabidopsis thaliana.
In: Nucleic acids research, Jg. 52 (2024-05-08), Heft 8, S. 4541-4555
academicJournal
Zugriff:
Formation of programmed DNA double-strand breaks is essential for initiating meiotic recombination. Genetic studies on Arabidopsis thaliana and Mus musculus have revealed that assembly of a type IIB topoisomerase VI (Topo VI)-like complex, composed of SPO11 and MTOPVIB, is a prerequisite for generating DNA breaks. However, it remains enigmatic if MTOPVIB resembles its Topo VI subunit B (VIB) ortholog in possessing robust ATPase activity, ability to undergo ATP-dependent dimerization, and activation of SPO11-mediated DNA cleavage. Here, we successfully prepared highly pure A. thaliana MTOPVIB and MTOPVIB-SPO11 complex. Contrary to expectations, our findings highlight that MTOPVIB differs from orthologous Topo VIB by lacking ATP-binding activity and independently forming dimers without ATP. Most significantly, our study reveals that while MTOPVIB lacks the capability to stimulate SPO11-mediated DNA cleavage, it functions as a bona fide DNA-binding protein and plays a substantial role in facilitating the dsDNA binding capacity of the MOTOVIB-SPO11 complex. Thus, we illustrate mechanistic divergence between the MTOPVIB-SPO11 complex and classical type IIB topoisomerases.
(© The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.)
Titel: |
Biochemical characterization of the meiosis-essential yet evolutionarily divergent topoisomerase VIB-like protein MTOPVIB from Arabidopsis thaliana.
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Autor/in / Beteiligte Person: | Chen, HW ; Yeh, HY ; Chang, CC ; Kuo, WC ; Lin, SW ; Vrielynck, N ; Grelon, M ; Chan, NL ; Chi, P |
Zeitschrift: | Nucleic acids research, Jg. 52 (2024-05-08), Heft 8, S. 4541-4555 |
Veröffentlichung: | 1992- : Oxford : Oxford University Press ; <i>Original Publication</i>: London, Information Retrieval ltd., 2024 |
Medientyp: | academicJournal |
ISSN: | 1362-4962 (electronic) |
DOI: | 10.1093/nar/gkae181 |
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