Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6YYL

Crystal structure of S. pombe Mei2 RRM3 domain

Summary for 6YYL
Entry DOI10.2210/pdb6yyl/pdb
DescriptorMeiosis protein mei2, DI(HYDROXYETHYL)ETHER, 1,2-ETHANEDIOL, ... (5 entities in total)
Functional Keywordsmeiosis rrm gene expression rna-binding domain, rna binding protein
Biological sourceSchizosaccharomyces pombe (strain 972 / ATCC 24843)
Total number of polymer chains2
Total formula weight42754.31
Authors
Graille, M.,Hazra, D. (deposition date: 2020-05-05, release date: 2020-12-23, Last modification date: 2024-05-15)
Primary citationAndric, 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: 33536434
DOI: 10.1038/s41467-021-21032-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.89 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon