Proceedings of the National Academy of Sciences · 2013 · 104 citations · 26 references
Life SciencesBiotechnologyMolecular BiologyGene ExpressionGenomicsTranscriptomicsCrispr-cas SystemsRna EditingCas Nuclease EngineeringCas Nuclease SpecificityHairpin MotifsRna-binding SpecificityTranscriptsWashing
RNA-binding proteins control the fate and function of the transcriptome in all cells. Here we present technology for isolating RNA-protein partners efficiently and accurately using an engineered clustered regularly interspaced short palindromic repeats (CRISPR) endoribonuclease. An inactive version of the Csy4 nuclease binds irreversibly to transcripts engineered with a 16-nt hairpin sequence at their 5' ends. Once immobilized by Csy4 on a solid support, contaminating proteins and other molecules can be removed by extensive washing. Upon addition of imidazole, Csy4 is activated to cleave the RNA, removing the hairpin tag and releasing the native transcript along with its specifically bound protein partners. This conditional Csy4 enzyme enables recovery of specific RNA-binding partners with minimal false-positive contamination. We use this method, coupled with quantitative MS, to identify cell type-specific human pre-microRNA-binding proteins. We also show that this technology is suitable for analyzing diverse size transcripts, and that it is suitable for adaptation to a high-throughput discovery format.
26
Universal sample preparation method for proteome analysis
Jacek R. Wiśniewski, Alexandre Zougman, Nagarjuna Nagaraj et al. · Nature Methods · 2009 · 8.7K citations
RAS Is Regulated by the let-7 MicroRNA Family
Steven Johnson, Jaclyn Shingara, Mike Byrom et al. · Cell · 2005 · 3.7K citations · Full text
Long Noncoding RNA as Modular Scaffold of Histone Modification Complexes
Miao-Chih Tsai, Ohad Manor, Yue Wan et al. · Science · 2010 · 3.3K citations · Full text
Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
Alfredo Castelló, Bernd Fischer, Katrin Eichelbaum et al. · Cell · 2012 · 2.3K citations · Full text