6HFG
Structure of the REC114 PH domain
Summary for 6HFG
| Entry DOI | 10.2210/pdb6hfg/pdb |
| Descriptor | Meiotic recombination protein REC114 (1 entity in total) |
| Functional Keywords | pleckstrin homology domain meiotic recombination, recombination |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 16239.39 |
| Authors | Juarez-Martinez, A.B.,de Massy, B.,Kadlec, J. (deposition date: 2018-08-21, release date: 2019-07-03, Last modification date: 2024-05-15) |
| Primary citation | Kumar, R.,Oliver, C.,Brun, C.,Juarez-Martinez, A.B.,Tarabay, Y.,Kadlec, J.,de Massy, B. Mouse REC114 is essential for meiotic DNA double-strand break formation and forms a complex with MEI4. Life Sci Alliance, 1:e201800259-e201800259, 2018 Cited by PubMed Abstract: Programmed formation of DNA double-strand breaks (DSBs) initiates the meiotic homologous recombination pathway. This pathway is essential for proper chromosome segregation at the first meiotic division and fertility. Meiotic DSBs are catalyzed by Spo11. Several other proteins are essential for meiotic DSB formation, including three evolutionarily conserved proteins first identified in (Mer2, Mei4, and Rec114). These three proteins and their mouse orthologs (IHO1, MEI4, and REC114) co-localize on the axes of meiotic chromosomes, and mouse IHO1 and MEI4 are essential for meiotic DSB formation. Here, we show that mouse is required for meiotic DSB formation. Moreover, MEI4 forms a complex with REC114 and IHO1 in mouse spermatocytes, consistent with cytological observations. We then demonstrated in vitro the formation of a stable complex between REC114 C-terminal domain and MEI4 N-terminal domain. We further determine the structure of the REC114 N-terminal domain that revealed similarity with Pleckstrin homology domains. These analyses provide direct insights into the architecture of these essential components of the meiotic DSB machinery. PubMed: 30569039DOI: 10.26508/lsa.201800259 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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