RtmR is a membrane-embedded RRM-family RNA-binding protein that regulates biofilm formation
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ABSTRACT:
PROVIDER: PRJNA1287783 | ENA |
REPOSITORIES: ENA
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Project description:RtmR is a membrane-embedded RRM-family RNA-binding protein
| PRJNA1490877 | ENA
Project description:The animal symbiont Vibrio fischeri has served as a model organism for molecular processes underlying bacterial group behaviors, including quorum sensing and biofilm development. Here, using a genetic approach to identify negative regulators of biofilm formation in V. fischeri, we identified a membrane-bound RNA-binding protein, RtmR (VF_2432), that acts as an inhibitor of the symbiosis polysaccharide (SYP) biofilm. Membrane localization of the protein seems to be required for protein stability, as truncation of the transmembrane helices led to an inability to detect the protein. The conserved RNP1 and RNP2 motifs in RtmR’s cytoplasmic RNA recognition motif (RRM) domain are required for function, and we demonstrate binding to RNA substrates. Identification of RtmR RNA ligands was conducted with a CLIP-seq approach that revealed a large interactome. One transcript identified was that of the biofilm regulatory histidine kinase RscS. We found that RtmR biofilm inhibition depends on RscS activity and that RtmR negatively regulates levels of RscS. Overall, this work characterizes a novel type of bacterial RNA-binding protein.
2025-07-09 | GSE301959 | GEO
Project description:The animal symbiont Vibrio fischeri has served as a model organism for molecular processes underlying bacterial group behaviors, including quorum sensing and biofilm development. Here, using a genetic approach to identify negative regulators of biofilm formation in V. fischeri, we identified a membrane-bound RNA-binding protein, RtmR (VF_2432), that acts as an inhibitor of the symbiosis polysaccharide (SYP) biofilm. Membrane localization of the protein seems to be required for protein stability or expression, as truncation of the transmembrane helices led to an inability to detect the protein. The conserved RNP1 and RNP2 motifs in RtmR’s cytoplasmic RNA recognition motif (RRM) domain are required for function, and we demonstrate binding to RNA substrates. Identification of RtmR RNA ligands was conducted with a iiCLIP-seq approach that revealed a large interactome. One transcript identified was that of the biofilm regulatory histidine kinase RscS. We found that RtmR biofilm inhibition depends on RscS activity and that RtmR negatively regulates levels of RscS. Overall, this work characterizes a novel type of bacterial RNA-binding protein.
2026-08-14 | GSE337776 | GEO
Project description: Not available
| S-EPMC12265689 | biostudies-literature
Project description:rs10-01_rrm - quadruple rrm experience - What is the role of the RRM protein family in plants? Plants were grown on soil in controlled environment under LD (16 h light/8 h dark) and the rosette leaves (8-leaf stage seedlings) were collected for RNA preparation. Keywords: normal vs transgenic comparison 2 dye-swap - CATMA arrays
2011-04-16 | E-GEOD-21701 | biostudies-arrayexpress
Project description:rs10-01_rrm - quadruple rrm experience - What is the role of the RRM protein family in plants? Plants were grown on soil in controlled environment under LD (16 h light/8 h dark) and the rosette leaves (8-leaf stage seedlings) were collected for RNA preparation. Keywords: normal vs transgenic comparison
2011-04-16 | GSE21701 | GEO
Project description:Screening of genes regulated between two grapevine genotypes (the Carignan and the RRM) during early inflorescence development
2009-12-08 | E-MEXP-1950 | biostudies-arrayexpress
Project description:membrane distillation biofilm Raw sequence reads
| PRJNA481855 | ENA
Project description:RNA-binding proteins (RBPs) are central players in determining the life cycle of RNA molecules. These proteins are often modular in arrangement, featuring multiple RNA-binding domains, to enhance RNA recognition and functionality. How these multiple RNA-binding domains within individual RBPs work in concert to recognize mRNA targets is still poorly studied. In the model fungus Ustilago maydis, the multi-RRM domain protein Rrm4 plays a key role in mediating the long-distance mRNA transport on the cytoplasmic surface of early endosomes, thereby precisely regulating spatiotemporal gene expression. Rrm4 contains three RNA-recognition motifs (RRMs), organized in an ELAV-like pattern: a tandem RRM domain (RRM1,2) and a separate third RRM domain (RRM3). Utilizing Rrm4 variants with mutations in the RRM domains, we conducted a differential iCLIP analysis to dissect the RNA recognition code of individual RRM domains. Our study reveals that Rrm4 exhibits two binding mode: (i) a one-to-one interaction where the third RRM domain alone binds RNAs by recognizing the shot UAUG motif. (ii) an intricate composite binding mode where all three RRM domains cooperatively bind RNA. Improtantly, our finding demonstrates that it is not the simple one-to-one interaction but rather the complex cooperative binding mode, involving all three RRM domains, is critical for Rrm4 function in maintaining the unipolar growth of the fungal hyphae.
2026-02-18 | GSE273495 | GEO
Project description:RNA-binding proteins (RBPs) are central players in determining the life cycle of RNA molecules. These proteins are often modular in arrangement, featuring multiple RNA-binding domains, to enhance RNA recognition and functionality. How these multiple RNA-binding domains within individual RBPs work in concert to recognize mRNA targets is still poorly studied. In the model fungus Ustilago maydis, the multi-RRM domain protein Rrm4 plays a key role in mediating the long-distance mRNA transport on the cytoplasmic surface of early endosomes, thereby precisely regulating spatiotemporal gene expression. Rrm4 contains three RNA-recognition motifs (RRMs), organized in an ELAV-like pattern: a tandem RRM domain (RRM1,2) and a separate third RRM domain (RRM3). Utilizing Rrm4 variants with mutations in the RRM domains, we conducted a differential iCLIP analysis to dissect the RNA recognition code of individual RRM domains. Our study reveals that Rrm4 exhibits two binding mode: (i) a one-to-one interaction where the third RRM domain alone binds RNAs by recognizing the shot UAUG motif. (ii) an intricate composite binding mode where all three RRM domains cooperatively bind RNA. Improtantly, our finding demonstrates that it is not the simple one-to-one interaction but rather the complex cooperative binding mode, involving all three RRM domains, is critical for Rrm4 function in maintaining the unipolar growth of the fungal hyphae.
2026-02-18 | GSE288123 | GEO