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An architectural role of specific RNA-RNA interactions in oskar granules.
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- Author(s): Bose M;Bose M;Bose M; Rankovic B; Rankovic B; Rankovic B; Mahamid J; Mahamid J; Mahamid J; Ephrussi A; Ephrussi A
- Source:
Nature cell biology [Nat Cell Biol] 2024 Nov; Vol. 26 (11), pp. 1934-1942. Date of Electronic Publication: 2024 Oct 01.- Publication Type:
Journal Article- Language:
English - Source:
- Additional Information
- Source: Publisher: Macmillan Magazines Ltd Country of Publication: England NLM ID: 100890575 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1476-4679 (Electronic) Linking ISSN: 14657392 NLM ISO Abbreviation: Nat Cell Biol Subsets: MEDLINE
- Publication Information: Original Publication: London : Macmillan Magazines Ltd., [1999-
- Subject Terms: Drosophila Proteins*/metabolism ; Drosophila Proteins*/genetics ; Drosophila melanogaster*/metabolism ; Drosophila melanogaster*/genetics ; RNA-Binding Proteins*/metabolism ; RNA-Binding Proteins*/genetics ; Oocytes*/metabolism ; Ribonucleoproteins*/metabolism ; Ribonucleoproteins*/genetics ; RNA, Messenger*/metabolism ; RNA, Messenger*/genetics ; Cytoplasmic Granules*/metabolism; Animals ; Female ; Mutation
- Abstract: Ribonucleoprotein (RNP) granules are membraneless condensates that organize the intracellular space by compartmentalization of specific RNAs and proteins. Studies have shown that RNA tunes the phase behaviour of RNA-binding proteins, but the role of intermolecular RNA-RNA interactions in RNP granules in vivo remains less explored. Here we determine the role of a sequence-specific RNA-RNA kissing-loop interaction in assembly of mesoscale oskar RNP granules in the female Drosophila germline. We show that a two-nucleotide mutation that disrupts kissing-loop-mediated oskar messenger RNA dimerization impairs condensate formation in vitro and oskar granule assembly in the developing oocyte, leading to defective posterior localization of the RNA and abrogation of oskar-associated processing bodies upon nutritional stress. This specific trans RNA-RNA interaction acts synergistically with the scaffold RNA-binding protein, Bruno, in driving condensate assembly. Our study highlights the architectural contribution of an mRNA and its specific secondary structure and tertiary interactions to the formation of an RNP granule that is essential for embryonic development.
Competing Interests: Competing interests The authors declare no competing interests.
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- Accession Number: 0 (Drosophila Proteins)
0 (osk protein, Drosophila)
0 (RNA-Binding Proteins)
0 (Ribonucleoproteins)
0 (RNA, Messenger)
0 (bru1 protein, Drosophila) - Publication Date: Date Created: 20241001 Date Completed: 20241116 Latest Revision: 20241120
- Publication Date: 20241120
- Accession Number: PMC11567897
- Accession Number: 10.1038/s41556-024-01519-3
- Accession Number: 39354131
- Source:
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