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P31comet, a member of the synaptonemal complex, participates in meiotic DSB formation in rice.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2016 Sep 20; Vol. 113 (38), pp. 10577-82. Date of Electronic Publication: 2016 Sep 06. - Publication Year :
- 2016
-
Abstract
- The human mitotic arrest-deficient 2 (Mad2) binding protein p31(comet) participates in the spindle checkpoint and coordinates cell cycle events in mitosis although its function in meiosis remains unknown in all organisms. Here, we reveal P31(comet) as a synaptonemal complex (SC) protein in rice (Oryza sativa L.). In p31(comet), homologous pairing and synapsis are eliminated, leading to the homologous nondisjunction and complete sterility. The failure in loading of histone H2AX phosphorylation (γH2AX) in p31(comet), together with the suppressed chromosome fragmentation in rice completion of meiotic recombination 1 (com1) p31(comet) and radiation sensitive 51c (rad51c) p31(comet) double mutants, indicates that P31(comet) plays an essential role in double-strand break (DSB) formation. Interestingly, the dynamic colocalization pattern between P31(comet) and ZEP1 (a transverse filament protein of SC) by immunostaining, as well as the interaction between P31(comet) and CENTRAL REGION COMPONENT 1 (CRC1) in yeast two-hybrid assays, suggests possible involvement of P31(comet) in SC installation. Together, these data indicate that P31(comet) plays a key role in DSB formation and SC installation, mainly through its cooperation with CRC1.<br />Competing Interests: The authors declare no conflict of interest.
- Subjects :
- Adaptor Proteins, Signal Transducing genetics
Cell Cycle Proteins genetics
DNA Breaks, Double-Stranded
M Phase Cell Cycle Checkpoints
Meiosis genetics
Mitosis genetics
Nuclear Proteins chemistry
Phosphorylation
Plant Proteins genetics
Spindle Apparatus genetics
Homologous Recombination genetics
Nuclear Proteins genetics
Oryza genetics
Synaptonemal Complex genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1091-6490
- Volume :
- 113
- Issue :
- 38
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 27601671
- Full Text :
- https://doi.org/10.1073/pnas.1607334113