Comprehensive analysis of diverse ribonucleoprotein complexes
Copyright policy )Comprehensive analysis of diverse ribonucleoprotein complexes
The study of the dynamic interactome of cellular ribonucleoprotein (RNP) particles has been hampered by severe methodological limitations. In particular, the affinity purification of intact RNP complexes from cell lysates suffers from RNA degradation, loss of interacting macromolecules and poor overall yields. Here we describe a rapid affinity-purification method for efficient isolation of the subcomplexes that dynamically organize different RNP biogenesis pathways in Saccharomyces cerevisiae. Our method overcomes many of the previous limitations to produce large RNP interactomes with almost no contamination.
- Rockefeller University United States
- Institute for Systems Biology United States
Ribosomal Proteins, Nucleocytoplasmic Transport Proteins, Saccharomyces cerevisiae Proteins, Green Fluorescent Proteins, Nuclear Proteins, Porins, RNA-Binding Proteins, RNA, Fungal, Saccharomyces cerevisiae, Mass Spectrometry, DNA-Binding Proteins, Ribonucleoproteins, RNA Cap-Binding Proteins, RNA, Ribosomal, Electrophoresis, Polyacrylamide Gel, RNA, Messenger, Staphylococcal Protein A, Immunosorbent Techniques, Oligonucleotide Array Sequence Analysis
Ribosomal Proteins, Nucleocytoplasmic Transport Proteins, Saccharomyces cerevisiae Proteins, Green Fluorescent Proteins, Nuclear Proteins, Porins, RNA-Binding Proteins, RNA, Fungal, Saccharomyces cerevisiae, Mass Spectrometry, DNA-Binding Proteins, Ribonucleoproteins, RNA Cap-Binding Proteins, RNA, Ribosomal, Electrophoresis, Polyacrylamide Gel, RNA, Messenger, Staphylococcal Protein A, Immunosorbent Techniques, Oligonucleotide Array Sequence Analysis
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