Proteomics

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A SUMO-Dependent Protein Network Regulates Chromosome Congression During Oocyte Meiosis


ABSTRACT: During Caenorhabditis elegans oocyte meiosis, a multi-protein complex localised between homologous chromosomes, the ring complex (RC), promotes chromosome congression through the action of the chromokinesin KLP-19. While some RC components are known, the mechanism of RC assembly has remained obscure. A germline-specific screen identified KLP-19 as a SUMO substrate in vivo and we found that the SUMO E3 ligase GEI-17/PIAS is required for KLP-19 recruitment to the RC. Additionally, KLP-19 is efficiently sumoylated in vitro in a GEI-17-dependent manner. Further biochemical analysis showed that KLP-19 and GEI-17 are efficiently modified by SUMO and that GEI-17 and another RC component, the kinase BUB-1, can interact non-covalently with SUMO. While SUMO conjugation is required for RC assembly, we also provide evidence consistent with non-covalent SUMO interactions contributing to RC assembly in vivo. Our results highlight the importance of sumoylation and non-covalent SUMO interaction in regulating dynamic protein complex assembly during oocyte meiosis.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Caenorhabditis Elegans

SUBMITTER: Triin Tammsalu  

LAB HEAD: Ronald T. Hay

PROVIDER: PXD005202 | Pride | 2020-10-15

REPOSITORIES: Pride

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Publications

A SUMO-Dependent Protein Network Regulates Chromosome Congression during Oocyte Meiosis.

Pelisch Federico F   Tammsalu Triin T   Wang Bin B   Jaffray Ellis G EG   Gartner Anton A   Hay Ronald T RT  

Molecular cell 20161208 1


During Caenorhabditis elegans oocyte meiosis, a multi-protein ring complex (RC) localized between homologous chromosomes, promotes chromosome congression through the action of the chromokinesin KLP-19. While some RC components are known, the mechanism of RC assembly has remained obscure. We show that SUMO E3 ligase GEI-17/PIAS is required for KLP-19 recruitment to the RC, and proteomic analysis identified KLP-19 as a SUMO substrate in vivo. In vitro analysis revealed that KLP-19 is efficiently s  ...[more]

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