Proteomics

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A quantitative proteomics approach to monitor targeted protein degradation in M. smegmatis

ABSTRACT: Targeted protein degradation via the ubiquitin proteasome has been established in eukaryotes, however no application has been shown in bacteria so far. In the present work, selective protein degradation is shown using hetero bifunctional drugs, bringing substrates in close proximity to the bacterial ClpC1P1P2 protein degradation complex. We performed a TMT based quantitative proteomics analysis to monitor degradation of human BRDT in Mycobacterium smegmatis. Our data shows selective degradation of BRDT when using bacterial PROTACS, indicating the first successful application of targeted protein degradation in bacteria.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Mycobacterium Smegmatis (strain Atcc 700084 / Mc(2)155) Bacteria

SUBMITTER: David Hoi  

LAB HEAD: Markus Hartl

PROVIDER: PXD021505 | Pride | 2022-08-12

REPOSITORIES: Pride

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Publications

Hijacking the cellular protein degradation system offers unique opportunities for drug discovery, as exemplified by proteolysis-targeting chimeras. Despite their great promise for medical chemistry, so far, it has not been possible to reprogram the bacterial degradation machinery to interfere with microbial infections. Here, we develop small-molecule degraders, so-called BacPROTACs, that bind to the substrate receptor of the ClpC:ClpP protease, priming neo-substrates for degradation. In addition  ...[more]

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