Corentin Claeys Bouuaert

This study investigates how Mer2 recruits Spp1 to form complexes involved in meiotic DSB machinery through structural and biochemical analysis.

This study identifies a conserved Red1 motif that interacts with Rec8 cohesin, promoting DSB formation and Mek1 activation during meiosis.

This study identifies mechanisms by which Mre11 is recruited during meiosis to initiate recombination in budding yeast.

The paper investigates Spo11 dimerization in S. cerevisiae, showing transient dimeric complexes and the role of Rec102 in DNA binding and dimerization.

This study shows that SPO11 dimerization is essential for meiotic DNA double-strand break formation, demonstrating that SPO11 can cleave DNA alone or with TOP6BL.

The paper reports cryo-EM structures of Spo11 core complexes bound to DNA, revealing DNA-binding specificity and structural variation in homologs.

The paper presents AlphaFold structures of Rec114-Mei4 and Mer2 complexes, showing their conserved structure across eukaryotes and DNA-binding properties.

The paper shows that DNA double-strand breaks (DSBs) during meiosis often occur in clusters with periodic spacing, challenging the idea that DSBs are isolated events.

This study characterizes the structure and function of the Spo11 core complex in S. cerevisiae, revealing its monomeric structure and DNA-binding properties related to meiotic DSB formation.

This study investigates how DNA-dependent macromolecular condensation facilitates the self-assembly of the meiotic DNA break machinery in yeast.

The paper identifies Dnmt3c as a fifth DNA methyltransferase paralog essential for retrotransposon methylation and male germline function in mice, revealing its role in meiosis and transposon repression.

This paper identifies distinct DNA-binding surfaces in MutLγ that mediate different functions in meiotic recombination and mismatch repair, revealing separable roles for Mlh1 and Mlh3.