The Axial Element Protein DESYNAPTIC2 Mediates Meiotic Double-Strand Break Formation and Synaptonemal Complex Assembly in Maize. Issue 9 (21st August 2015)
- Record Type:
- Journal Article
- Title:
- The Axial Element Protein DESYNAPTIC2 Mediates Meiotic Double-Strand Break Formation and Synaptonemal Complex Assembly in Maize. Issue 9 (21st August 2015)
- Main Title:
- The Axial Element Protein DESYNAPTIC2 Mediates Meiotic Double-Strand Break Formation and Synaptonemal Complex Assembly in Maize
- Authors:
- Lee, Ding Hua
Kao, Yu-Hsin
Ku, Jia-Chi
Lin, Chien-Yu
Meeley, Robert
Jan, Ya-Shiun
Wang, Chung-Ju Rachel - Abstract:
- Abstract : Maize DSY2 mediates DNA double-strand-break formation to initiate recombination and connects the axial element with the central element protein ZYP1 during synapsis. Abstract: During meiosis, homologous chromosomes pair and recombine via repair of programmed DNA double-strand breaks (DSBs ). DSBs are formed in the context of chromatin loops, which are anchored to the proteinaceous axial element (AE ). The AE later serves as a framework to assemble the synaptonemal complex (SC ) that provides a transient but tight connection between homologous chromosomes. Here, we showed that DESYNAPTIC2 (DSY2), a coiled-coil protein, mediates DSB formation and is directly involved in SC assembly in maize ( Zea mays ). The dsy2 mutant exhibits homologous pairing defects, leading to sterility. Analyses revealed that DSB formation and the number of RADIATION SENSITIVE51 (RAD51) foci are largely reduced, and synapsis is completely abolished in dsy2 meiocytes. Super-resolution structured illumination microscopy showed that DSY2 is located on the AE and forms a distinct alternating pattern with the HORMA-domain protein ASYNAPTIC1 (ASY1). In the dsy2 mutant, localization of ASY1 is affected, and loading of the central element ZIPPER1 (ZYP1) is disrupted. Yeast two-hybrid and bimolecular fluorescence complementation experiments further demonstrated that ZYP1 interacts with DSY2 but does not interact with ASY1. Therefore, DSY2, an AE protein, not only mediates DSB formation but alsoAbstract : Maize DSY2 mediates DNA double-strand-break formation to initiate recombination and connects the axial element with the central element protein ZYP1 during synapsis. Abstract: During meiosis, homologous chromosomes pair and recombine via repair of programmed DNA double-strand breaks (DSBs ). DSBs are formed in the context of chromatin loops, which are anchored to the proteinaceous axial element (AE ). The AE later serves as a framework to assemble the synaptonemal complex (SC ) that provides a transient but tight connection between homologous chromosomes. Here, we showed that DESYNAPTIC2 (DSY2), a coiled-coil protein, mediates DSB formation and is directly involved in SC assembly in maize ( Zea mays ). The dsy2 mutant exhibits homologous pairing defects, leading to sterility. Analyses revealed that DSB formation and the number of RADIATION SENSITIVE51 (RAD51) foci are largely reduced, and synapsis is completely abolished in dsy2 meiocytes. Super-resolution structured illumination microscopy showed that DSY2 is located on the AE and forms a distinct alternating pattern with the HORMA-domain protein ASYNAPTIC1 (ASY1). In the dsy2 mutant, localization of ASY1 is affected, and loading of the central element ZIPPER1 (ZYP1) is disrupted. Yeast two-hybrid and bimolecular fluorescence complementation experiments further demonstrated that ZYP1 interacts with DSY2 but does not interact with ASY1. Therefore, DSY2, an AE protein, not only mediates DSB formation but also bridges the AE and central element of SC during meiosis. … (more)
- Is Part Of:
- The Plant Cell. Volume 27:Issue 9(2015)
- Journal:
- The Plant Cell
- Issue:
- Volume 27:Issue 9(2015)
- Issue Display:
- Volume 27, Issue 9 (2015)
- Year:
- 2015
- Volume:
- 27
- Issue:
- 9
- Issue Sort Value:
- 2015-0027-0009-0000
- Page Start:
- 2516
- Page End:
- 2529
- Publication Date:
- 2015-08-21
- Journal URLs:
- http://www.oxfordjournals.org/ ↗
- DOI:
- 10.1105/tpc.15.00434 ↗
- Languages:
- English
- ISSNs:
- 1040-4651
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16352.xml