Proteomics

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Proteomic Analysis of RAP (RNA Antisense Purification) isolated RNPs (RiboNucleotide Particles) harboring the novel lncRNA mimi


ABSTRACT: In neurons, mRNAs and associated RNA-binding proteins assemble into ribonucleoprotein (RNP) granules essential to regulate mRNA trafficking, local translation, and turnover. Dysregulation of RNA-protein condensation can disturb synaptic plasticity. We report that the novel lncRNA mimi is a constitutive and essential component of large cytoplasmic condensates (RNP granules) in fly neurons. In order to identify direct mimi RNA binders we employ RAP assisted purification of mimi RNPs subsequent to UV-crosslinking of adult fly brain tissue (non UV irradiated samples serve as control). Applying relative Max Quant LFQ quantification (Max LFQ) we carry out a differential proteomic analysis of mimi RNP complexes in UV-irradiated versus non irradiated fly brains.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

TISSUE(S): Brain

SUBMITTER: Gerhard Mittler  

LAB HEAD: Gerhard Mittler

PROVIDER: PXD034457 | Pride | 2022-10-12

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
00000780___S01_inj01.raw Raw
00000780___S01_inj02.raw Raw
00000781___S02_inj01.raw Raw
00000781___S02_inj02.raw Raw
00000782___S03_inj01.raw Raw
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Publications


RNA binding proteins and messenger RNAs (mRNAs) assemble into ribonucleoprotein granules that regulate mRNA trafficking, local translation, and turnover. The dysregulation of RNA-protein condensation disturbs synaptic plasticity and neuron survival and has been widely associated with human neurological disease. Neuronal granules are thought to condense around particular proteins that dictate the identity and composition of each granule type. Here, we show in <i>Drosophila</i> that a previously u  ...[more]

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