6YYL
Crystal structure of S. pombe Mei2 RRM3 domain
Summary for 6YYL
Entry DOI | 10.2210/pdb6yyl/pdb |
Descriptor | Meiosis protein mei2, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (5 entities in total) |
Functional Keywords | meiosis rrm gene expression rna-binding domain, rna binding protein |
Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) |
Total number of polymer chains | 2 |
Total formula weight | 42754.31 |
Authors | Graille, M.,Hazra, D. (deposition date: 2020-05-05, release date: 2020-12-23, Last modification date: 2024-05-15) |
Primary citation | Andric, V.,Nevers, A.,Hazra, D.,Auxilien, S.,Menant, A.,Graille, M.,Palancade, B.,Rougemaille, M. A scaffold lncRNA shapes the mitosis to meiosis switch. Nat Commun, 12:770-770, 2021 Cited by PubMed Abstract: Long non-coding RNAs (lncRNAs) contribute to the regulation of gene expression in response to intra- or extracellular signals but the underlying molecular mechanisms remain largely unexplored. Here, we identify an uncharacterized lncRNA as a central player in shaping the meiotic gene expression program in fission yeast. We report that this regulatory RNA, termed mamRNA, scaffolds the antagonistic RNA-binding proteins Mmi1 and Mei2 to ensure their reciprocal inhibition and fine tune meiotic mRNA degradation during mitotic growth. Mechanistically, mamRNA allows Mmi1 to target Mei2 for ubiquitin-mediated downregulation, and conversely enables accumulating Mei2 to impede Mmi1 activity, thereby reinforcing the mitosis to meiosis switch. These regulations also occur within a unique Mmi1-containing nuclear body, positioning mamRNA as a spatially-confined sensor of Mei2 levels. Our results thus provide a mechanistic basis for the mutual control of gametogenesis effectors and further expand our vision of the regulatory potential of lncRNAs. PubMed: 33536434DOI: 10.1038/s41467-021-21032-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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