Structural highlights
Function[PCH2_CAEEL] Plays a key role in chromosome recombination during meiosis. Publication Abstract from PubMedThe AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family. Here we present the structure of the C. elegans TRIP13 ortholog PCH-2, revealing a new family of AAA+ ATPase protein remodelers. PCH-2 possesses a substrate-recognition domain related to those of the protein remodelers NSF and p97, while its overall hexameric architecture and likely structural mechanism bear close similarities to the bacterial protein unfoldase ClpX. We find that TRIP13, aided by the adapter protein p31(comet), converts the HORMA-family spindle checkpoint protein MAD2 from a signaling-active 'closed' conformer to an inactive 'open' conformer. We propose that TRIP13 and p31(comet) collaborate to inactivate the spindle assembly checkpoint through MAD2 conformational conversion and disassembly of mitotic checkpoint complexes. A parallel HORMA protein disassembly activity likely underlies TRIP13's critical regulatory functions in meiotic chromosome structure and recombination. TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching.,Ye Q, Rosenberg SC, Moeller A, Speir JA, Su TY, Corbett KD Elife. 2015 Apr 28;4. doi: 10.7554/eLife.07367. PMID:25918846[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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