Mechanism and Control of Meiotic DNA Double-Strand Break Formation in S. cerevisiae

Yadav, Vikash Kumar; Bouuaert, Corentin Claeys

doi:10.3389/fcell.2021.642737

Cited by 49 publications

(53 citation statements)

References 210 publications

(349 reference statements)

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“…This is, for example, the case of the recently identified mammalian protein ANKRD31 ( 36 , 37 ) and the A. thaliana DFO protein ( 38 ). The function of these DSB proteins during meiotic DSB formation is still largely unknown ( 5 , 8 , 28 ), but they could act as regulators of either the formation or the activation of the catalytic core complex, to trigger DSB formation in a timely and accurately regulated manner.…”

Section: Introductionmentioning

confidence: 99%

Conservation and divergence of meiotic DNA double strand break forming mechanisms in Arabidopsis thaliana

Vrielynck

Schneider

Rodriguez

et al. 2021

Nucleic Acids Research

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In the current meiotic recombination initiation model, the SPO11 catalytic subunits associate with MTOPVIB to form a Topoisomerase VI-like complex that generates DNA double strand breaks (DSBs). Four additional proteins, PRD1/AtMEI1, PRD2/AtMEI4, PRD3/AtMER2 and the plant specific DFO are required for meiotic DSB formation. Here we show that (i) MTOPVIB and PRD1 provide the link between the catalytic sub-complex and the other DSB proteins, (ii) PRD3/AtMER2, while localized to the axis, does not assemble a canonical pre-DSB complex but establishes a direct link between the DSB-forming and resection machineries, (iii) DFO controls MTOPVIB foci formation and is part of a divergent RMM-like complex including PHS1/AtREC114 and PRD2/AtMEI4 but not PRD3/AtMER2, (iv) PHS1/AtREC114 is absolutely unnecessary for DSB formation despite having a conserved position within the DSB protein network and (v) MTOPVIB and PRD2/AtMEI4 interact directly with chromosome axis proteins to anchor the meiotic DSB machinery to the axis.

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Section: Introductionmentioning

confidence: 99%

Conservation and divergence of meiotic DNA double strand break forming mechanisms in Arabidopsis thaliana

Vrielynck

Schneider

Rodriguez

et al. 2021

Nucleic Acids Research

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show abstract

“…Crossover resolution involves Mlh1. Other proteins have also been shown to act in meiotic recombination in mammals (reviewed inBaudat et al, 2013) and in budding yeast (reviewed inYadav and Claeys Bouuaert, 2021). Presented proteins have been studied in zebrafish by mutation and/or cytological analyses.…”

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confidence: 99%

Meiotic Chromosome Dynamics in Zebrafish

Imai

Olaya

Sakai

et al. 2021

Front. Cell Dev. Biol.

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Recent studies in zebrafish have revealed key features of meiotic chromosome dynamics, including clustering of telomeres in the bouquet configuration, biogenesis of chromosome axis structures, and the assembly and disassembly of the synaptonemal complex that aligns homologs end-to-end. The telomere bouquet stage is especially pronounced in zebrafish meiosis and sub-telomeric regions play key roles in mediating pairing and homologous recombination. In this review, we discuss the temporal progression of these events in meiosis prophase I and highlight the roles of proteins associated with meiotic chromosome architecture in homologous recombination. Finally, we discuss the interplay between meiotic mutants and gonadal sex differentiation and future research directions to study meiosis in living cells, including cell culture.

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“…Hop1 and Red1 play a role in DSB formation by serving as a platform for the Mer2/Mei4/Rec114 DSB proteins ( Panizza et al, 2011 ; Figure 2 ) that then promote Spo11 catalytic activity through direct or indirect interactions with Spo11 ( Yadav and Claeys Bouuaert, 2021 ). This Hop1/Red1 function is mediated by the direct interaction between Hop1 and Mer2 in S. cerevisiae ( Rousova et al, 2020 ), and between their orthologs Hop1 and Rec15 in S. pombe ( Kariyazono et al, 2019 ).…”

Section: Organization Of the Chromosome Axial Element In S Cerevisiaementioning

confidence: 99%

Chromosome Organization in Early Meiotic Prophase

Grey

Massy

2021

Front. Cell Dev. Biol.

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One of the most fascinating aspects of meiosis is the extensive reorganization of the genome at the prophase of the first meiotic division (prophase I). The first steps of this reorganization are observed with the establishment of an axis structure, that connects sister chromatids, from which emanate arrays of chromatin loops. This axis structure, called the axial element, consists of various proteins, such as cohesins, HORMA-domain proteins, and axial element proteins. In many organisms, axial elements are required to set the stage for efficient sister chromatid cohesion and meiotic recombination, necessary for the recognition of the homologous chromosomes. Here, we review the different actors involved in axial element formation in Saccharomyces cerevisiae and in mouse. We describe the current knowledge of their localization pattern during prophase I, their functional interdependence, their role in sister chromatid cohesion, loop axis formation, homolog pairing before meiotic recombination, and recombination. We also address further challenges that need to be resolved, to fully understand the interplay between the chromosome structure and the different molecular steps that take place in early prophase I, which lead to the successful outcome of meiosis I.

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Mechanism and Control of Meiotic DNA Double-Strand Break Formation in S. cerevisiae

Cited by 49 publications

References 210 publications

Conservation and divergence of meiotic DNA double strand break forming mechanisms in Arabidopsis thaliana

Conservation and divergence of meiotic DNA double strand break forming mechanisms in Arabidopsis thaliana

Meiotic Chromosome Dynamics in Zebrafish

Chromosome Organization in Early Meiotic Prophase

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