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SORTing out cellular proteomes in vivo

Nature Biotechnology volume 32, pages 445–446 (2014)Cite this article

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Incorporation of a new unnatural amino acid during protein synthesis enables proteomic profiling of specific cell types in whole animals.

Methods for analyzing whole proteomes have revealed mechanisms of cell signaling and protein synthesis1, but these approaches typically require ex vivo purification of specific cell populations from whole animals. In this issue, Elliott et al.2 address this limitation with a new technology called stochastic orthogonal recoding of translation with chemoselective modification (SORT-M). SORT-M uses a set of reengineered orthogonal pyrrolysyl-tRNA synthetase/tRNA pairs that enables codon-selective incorporation of a cyclopropene lysine derivative, which can be chemoselectively modified with various tetrazine probes for fluorescence imaging and proteome profiling of engineered bacteria, mammalian cells and specific cell types or tissues in animals. SORT-M thus provides new opportunities to analyze global protein expression in genetically targeted cell populations in whole animals in a variety of biological settings.

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Figure 1: SORT-M technology for labeling the proteome of specific cells in a whole animal.

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Authors and Affiliations

  1. Tao Peng and Howard C. Hang are at the Laboratory of Chemical Biology and Microbial Pathogenesis, The Rockefeller University, New York, New York, USA.,

    Tao Peng & Howard C Hang

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  1. Tao Peng
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  2. Howard C Hang
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Correspondence to Howard C Hang.

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The authors declare no competing financial interests.

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Peng, T., Hang, H. SORTing out cellular proteomes in vivo. Nat Biotechnol 32, 445–446 (2014). https://doi.org/10.1038/nbt.2898

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