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A SUMO-ubiquitin relay recruits proteasomes to chromosome axes to regulate meiotic recombination.


ABSTRACT: Meiosis produces haploid gametes through a succession of chromosomal events, including pairing, synapsis, and recombination. Mechanisms that orchestrate these events remain poorly understood. We found that the SUMO (small ubiquitin-like modifier)-modification and ubiquitin-proteasome systems regulate the major events of meiotic prophase in mouse. Interdependent localization of SUMO, ubiquitin, and proteasomes along chromosome axes was mediated largely by RNF212 and HEI10, two E3 ligases that are also essential for crossover recombination. RNF212-dependent SUMO conjugation effected a checkpointlike process that stalls recombination by rendering the turnover of a subset of recombination factors dependent on HEI10-mediated ubiquitylation. We propose that SUMO conjugation establishes a precondition for designating crossover sites via selective protein stabilization. Thus, meiotic chromosome axes are hubs for regulated proteolysis via SUMO-dependent control of the ubiquitin-proteasome system.

SUBMITTER: Rao HB 

PROVIDER: S-EPMC5569317 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

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A SUMO-ubiquitin relay recruits proteasomes to chromosome axes to regulate meiotic recombination.

Rao H B D Prasada HB   Qiao Huanyu H   Bhatt Shubhang K SK   Bailey Logan R J LR   Tran Hung D HD   Bourne Sarah L SL   Qiu Wendy W   Deshpande Anusha A   Sharma Ajay N AN   Beebout Connor J CJ   Pezza Roberto J RJ   Hunter Neil N  

Science (New York, N.Y.) 20170105 6323


Meiosis produces haploid gametes through a succession of chromosomal events, including pairing, synapsis, and recombination. Mechanisms that orchestrate these events remain poorly understood. We found that the SUMO (small ubiquitin-like modifier)-modification and ubiquitin-proteasome systems regulate the major events of meiotic prophase in mouse. Interdependent localization of SUMO, ubiquitin, and proteasomes along chromosome axes was mediated largely by RNF212 and HEI10, two E3 ligases that are  ...[more]

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