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<p>The meiotic chromosome axis organizes chromatin and sets the stage for homolog pairing and recombination. <Emphasis Type="Underline">M</Emphasis>eiotic <Emphasis Type="Underline">HORMA d</Emphasis>omain proteins (mHORMADs) are conserved axis components that conformationally transform during target binding. In <i>C. elegans</i>, four functionally distinct mHORMADs directly interact, but how binding between them is restricted to axis assembly is unknown. Using a mutation in the mHORMADs that delays axis assembly, we isolated a suppressor mutation in a TRiC (<Emphasis Type="Underline">T</Emphasis>ailless complex peptide 1 <Emphasis Type="Underline">Ri</Emphasis>ng <Emphasis Type="Underline">C</Emphasis>omplex) chaperonin subunit that restored mHORMAD localization. CCT-4 associates with meiotic chromatin and forms in vivo complexes with mHORMADs, while germline disruption of TRiC results in axis defects, indicating a nuclear function for TRiC alongside meiotic chromosomes. We propose that chromosome-associated TRiC locally folds mHORMADs into the binding-competent conformation required for axis morphogenesis. More broadly, our results support the model that spatially-restricted folding by TRiC/CCT is a mechanism of controlling the assembly of multimeric complexes that function in tightly co-ordinated events.</p>

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A nuclear TRiC/CCT chaperonin assembles meiotic HORMAD proteins into chromosome axes competent for crossing over

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年10月24日

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  • Monique Zetka,
  • Amirhossein Pezeshki,
  • Ryan Dawson,
  • Pim J. Huis In ’t Veld,
  • Steven J. M. Jones,
  • Nicola Silva

摘要

The meiotic chromosome axis organizes chromatin and sets the stage for homolog pairing and recombination. Meiotic HORMA domain proteins (mHORMADs) are conserved axis components that conformationally transform during target binding. In C. elegans, four functionally distinct mHORMADs directly interact, but how binding between them is restricted to axis assembly is unknown. Using a mutation in the mHORMADs that delays axis assembly, we isolated a suppressor mutation in a TRiC (Tailless complex peptide 1 Ring Complex) chaperonin subunit that restored mHORMAD localization. CCT-4 associates with meiotic chromatin and forms in vivo complexes with mHORMADs, while germline disruption of TRiC results in axis defects, indicating a nuclear function for TRiC alongside meiotic chromosomes. We propose that chromosome-associated TRiC locally folds mHORMADs into the binding-competent conformation required for axis morphogenesis. More broadly, our results support the model that spatially-restricted folding by TRiC/CCT is a mechanism of controlling the assembly of multimeric complexes that function in tightly co-ordinated events.