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Proper chromosome segregation during meiosis requires the assembly of the synaptonemal complex (SC) between homologous chromosomes. However, the SC structure itself is indifferent to homology, and poorly understood mechanisms that depend on conserved HORMA-domain proteins prevent ectopic SC assembly. Although HORMA-domain proteins are thought to regulate SC assembly as intrinsic components of meiotic chromosomes, here we uncover a key role for nuclear soluble HORMA-domain protein HTP-1 in the quality control of SC assembly. We show that a mutant form of HTP-1 impaired in chromosome loading provides functionality of an HTP-1-dependent checkpoint that delays exit from homology search-competent stages until all homolog pairs are linked by the SC. Bypassing of this regulatory mechanism results in premature meiotic progression and licensing of homology-independent SC assembly. These findings identify nuclear soluble HTP-1 as a regulator of early meiotic progression, suggesting parallels with the mode of action of Mad2 in the spindle assembly checkpoint.

Original publication

DOI

10.1016/j.devcel.2014.10.001

Type

Journal article

Journal

Dev Cell

Publication Date

24/11/2014

Volume

31

Pages

503 - 511

Keywords

Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cell Cycle Proteins, Chromosome Pairing, Chromosome Segregation, Meiosis, Signal Transduction, Synaptonemal Complex