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• W2044388511 abstract "•HORMA proteins play central but mysterious roles in meiotic chromosome metabolism •In C. elegans and mammals, HORMA proteins assemble through head-to-tail interactions •Hierarchical assembly of HORMA domain proteins underlies chromosome axis structure •Disruption of specific binding interactions allows targeted analysis in vivo Proteins of the HORMA domain family play central, but poorly understood, roles in chromosome organization and dynamics during meiosis. In Caenorhabditis elegans, four such proteins (HIM-3, HTP-1, HTP-2, and HTP-3) have distinct but overlapping functions. Through combined biochemical, structural, and in vivo analysis, we find that these proteins form hierarchical complexes through binding of their HORMA domains to cognate peptides within their partners’ C-terminal tails, analogous to the “safety belt” binding mechanism of Mad2. These interactions are critical for recruitment of HIM-3, HTP-1, and HTP-2 to chromosome axes. HTP-3, in addition to recruiting the other HORMA domain proteins to the axis, plays an independent role in sister chromatid cohesion and double-strand break formation. Finally, we find that mammalian HORMAD1 binds a motif found both at its own C terminus and at that of HORMAD2, indicating that this mode of intermolecular association is a conserved feature of meiotic chromosome structure in eukaryotes. Proteins of the HORMA domain family play central, but poorly understood, roles in chromosome organization and dynamics during meiosis. In Caenorhabditis elegans, four such proteins (HIM-3, HTP-1, HTP-2, and HTP-3) have distinct but overlapping functions. Through combined biochemical, structural, and in vivo analysis, we find that these proteins form hierarchical complexes through binding of their HORMA domains to cognate peptides within their partners’ C-terminal tails, analogous to the “safety belt” binding mechanism of Mad2. These interactions are critical for recruitment of HIM-3, HTP-1, and HTP-2 to chromosome axes. HTP-3, in addition to recruiting the other HORMA domain proteins to the axis, plays an independent role in sister chromatid cohesion and double-strand break formation. Finally, we find that mammalian HORMAD1 binds a motif found both at its own C terminus and at that of HORMAD2, indicating that this mode of intermolecular association is a conserved feature of meiotic chromosome structure in eukaryotes. HORMA Domains at the Heart of Meiotic Chromosome DynamicsVader et al.Developmental CellNovember 24, 2014In BriefHORMA domain proteins are required for the careful orchestration of chromosomal organization during meiosis. Kim et al. (2014) and Silva et al. (2014) now provide structural and functional insights into the roles of C. elegans HORMA proteins, revealing parallels to the function of the HORMA protein MAD2 in mitotic checkpoint signaling. Full-Text PDF Open ArchiveThe Fidelity of Synaptonemal Complex Assembly Is Regulated by a Signaling Mechanism that Controls Early Meiotic ProgressionSilva et al.Developmental CellNovember 6, 2014In BriefSilva et al. examine quality control of synaptonemal complex (SC) assembly during meiosis, as implemented by a prophase checkpoint. They find that signaling by a soluble pool of the HORMA-domain protein HTP-1 controls this checkpoint and thus prevents improper SC assembly, independent of HTP-1 loading and function at axial elements. Full-Text PDF" @default.
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• W2044388511 date "2014-11-01" @default.
• W2044388511 modified "2023-10-16" @default.
• W2044388511 title "The Chromosome Axis Controls Meiotic Events through a Hierarchical Assembly of HORMA Domain Proteins" @default.
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• W2044388511 doi "https://doi.org/10.1016/j.devcel.2014.09.013" @default.
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