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Cellular thermal shift analysis for interrogation of CRISPR-assisted proteomic changes.

Nam-Gu Her1,2, Ivan Babic3, Venkata M Yenugonda3

  • 1Korea Institute of Radiological & Medical Sciences, Nowon, Seoul 01812, Korea.

Biotechniques
|February 11, 2020
PubMed
Summary

CRISPR-Cas9 gene editing enables dense mutagenesis to identify disease-related genes. A new method links these genetic changes to protein alterations, aiding therapeutic modulator discovery for complexes like NuRD.

Keywords:
CETSACRISPRcellular thermal shiftprotein complex

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Area of Science:

  • Genomics and Proteomics
  • Molecular Biology
  • Epigenetics

Background:

  • CRISPR-Cas9 is a powerful tool for genetic element discovery in diseases.
  • Perturbing protein-coding sequences in situ aids in identifying therapeutic targets.
  • Linking genomics data to cellular proteomics is crucial but challenging.

Purpose of the Study:

  • To develop a method for interrogating proteomic shifts from CRISPR-assisted dense mutagenesis.
  • To establish a link between genetic perturbations and proteomic changes in cells.
  • To apply this method to study the NuRD epigenetic complex.

Main Methods:

  • CRISPR-assisted dense mutagenesis to perturb protein-coding sequences.
  • Cellular thermal shift assays (CETSA) to measure proteomic changes.
  • Application of the method to the NuRD epigenetic complex.

Main Results:

  • Successfully integrated CRISPR-based mutagenesis with proteomic analysis.
  • Demonstrated the ability to interrogate proteomic shifts in response to genetic perturbations.
  • Provided a case study on the NuRD epigenetic complex.

Conclusions:

  • The developed method bridges the gap between genomics and proteomics for disease-related gene discovery.
  • This approach facilitates the identification of modulators for challenging therapeutic targets.
  • The study highlights the utility of combining CRISPR mutagenesis with CETSA for biological insights.