Control of meiotic crossover interference by a proteolytic chaperone network

A - Papers appearing in refereed journals

Kim, H., Kim, J., Son, N., Kuo, P., Morgan, C., Chambon, A., Byun, D., Park, J., Lee, Y., Park, Y. M., Fozard, J. A., Guerin, J., Hurel, A., Lambing, C., Howard, M., Hwang, I., Mercier, R., Grelon, M., Henderson, I. R. and Choi, K. 2024. Control of meiotic crossover interference by a proteolytic chaperone network. Nature Plants. https://doi.org/10.1038/s41477-024-01633-y

AuthorsKim, H., Kim, J., Son, N., Kuo, P., Morgan, C., Chambon, A., Byun, D., Park, J., Lee, Y., Park, Y. M., Fozard, J. A., Guerin, J., Hurel, A., Lambing, C., Howard, M., Hwang, I., Mercier, R., Grelon, M., Henderson, I. R. and Choi, K.
Abstract

Meiosis is a specialized eukaryotic division that produces genetically diverse gametes for sexual reproduction. During meiosis, homologous chromosomes pair and undergo reciprocal exchanges, called crossovers, which recombine genetic variation. Meiotic crossovers are stringently controlled with at least one obligate exchange forming per chromosome pair, while closely spaced crossovers are inhibited by interference. In Arabidopsis, crossover positions can be explained by a diffusion-mediated coarsening model, in which large, approximately evenly spaced foci of the pro-crossover E3 ligase HEI10 grow at the expense of smaller, closely spaced clusters. However, the mechanisms that control HEI10 dynamics during meiosis remain unclear. Here, through a forward genetic screen in Arabidopsis, we identified high crossover rate3 (hcr3), a dominant-negative mutant that reduces crossover interference and increases crossovers genome-wide. HCR3 encodes J3, a co-chaperone related to HSP40, which acts to target protein aggregates and biomolecular condensates to the disassembly chaperone HSP70, thereby promoting proteasomal degradation. Consistently, we show that a network of HCR3 and HSP70 chaperones facilitates proteolysis of HEI10, thereby regulating interference and the recombination landscape. These results reveal a new role for the HSP40/J3-HSP70 chaperones in regulating chromosome-wide dynamics of recombination via control of HEI10 proteolysis.

Year of Publication2024
JournalNature Plants
Digital Object Identifier (DOI)https://doi.org/10.1038/s41477-024-01633-y
Web address (URL)https://www.nature.com/articles/s41477-024-01633-y
Open accessPublished as non-open access
FunderBiotechnology and Biological Sciences Research Council
Funder project or codeDelivering Sustainable Wheat
Output statusPublished
Publication dates
Online20 Feb 2024
Publication process dates
Accepted24 Jan 2024
PublisherNature Publishing Group
ISSN2055-026X

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