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

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.