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De novo identification of essential protein domains from CRISPR-Cas9 tiling-sgRNA knockout screens

High-throughput CRISPR-Cas9 knockout screens using a tiling-sgRNA design permit in situ evaluation of protein domain function. Here, to facilitate de novo identification of essential protein domains from such screens, we propose ProTiler, a computational method for the robust mapping of CRISPR knock...

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Detalles Bibliográficos
Autores principales: He, Wei, Zhang, Liang, Villarreal, Oscar D., Fu, Rongjie, Bedford, Ella, Dou, Jingzhuang, Patel, Anish Y., Bedford, Mark T., Shi, Xiaobing, Chen, Taiping, Bartholomew, Blaine, Xu, Han
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6778102/
https://www.ncbi.nlm.nih.gov/pubmed/31586052
http://dx.doi.org/10.1038/s41467-019-12489-8
Descripción
Sumario:High-throughput CRISPR-Cas9 knockout screens using a tiling-sgRNA design permit in situ evaluation of protein domain function. Here, to facilitate de novo identification of essential protein domains from such screens, we propose ProTiler, a computational method for the robust mapping of CRISPR knockout hyper-sensitive (CKHS) regions, which refer to the protein regions associated with a strong sgRNA dropout effect in the screens. Applied to a published CRISPR tiling screen dataset, ProTiler identifies 175 CKHS regions in 83 proteins. Of these CKHS regions, more than 80% overlap with annotated Pfam domains, including all of the 15 known drug targets in the dataset. ProTiler also reveals unannotated essential domains, including the N-terminus of the SWI/SNF subunit SMARCB1, which is validated experimentally. Surprisingly, the CKHS regions are negatively correlated with phosphorylation and acetylation sites, suggesting that protein domains and post-translational modification sites have distinct sensitivities to CRISPR-Cas9 mediated amino acids loss.