한빛사논문
- 조회469
Heejin Kim1,7, Jaeil Kim1,7, Namil Son1, Pallas Kuo 2,3, Chris Morgan 4, Aurélie Chambon5, Dohwan Byun1, Jihye Park1, Youngkyung Lee1, Yeong Mi Park1, John A. Fozard4, Julie Guérin5, Aurélie Hurel5, Christophe Lambing2,3, Martin Howard4, Ildoo Hwang1, Raphael Mercier6, Mathilde Grelon5, Ian R. Henderson2 & Kyuha Choi1
1Department of Life Sciences, Pohang University of Science and Technology, Pohang, Republic of Korea.
2Department of Plant Sciences, University of Cambridge, Cambridge, UK.
3Rothamsted Research, Harpenden, UK.
4John Innes Centre, Norwich Research Park, Norwich, UK.
5Institut Jean-Pierre Bourgin (IJPB), Université Paris-Saclay, INRAE, AgroParisTech, Versailles, France.
6Department of Chromosome Biology, Max Planck Institute for Plant Breeding Research, Cologne, Germany.
7These authors contributed equally: Heejin Kim, Jaeil Kim.
Corresponding author : Correspondence to Kyuha Choi.
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.
논문정보
- Research article
- 2024년 02월 (BRIC 등록일 2024-02-22)
- 국내(교신)+국외 연구진
- 생명과학 > 식물학
관련 보도자료
- Bio통신원
- 2024. 02. 28
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