ArticlePloS one2014
Bacterial proteasome activator bpa (rv3780) is a novel ring-shaped interactor of the mycobacterial proteasome.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 39 citations in OpenAlex.
- Fred Goldberg machines in the pathogenesis of Mycobacterium tuberculosis.The Journal of biological chemistry · 2026Review
- Structural heterogeneity and substrate engagement mechanism of the bacterial proteasome activator Bpa.Nature communications · 2026Article
- Real-time capture of σNature communications · 2025Article
- "Pupdates" on proteasomal degradation in bacteria.Journal of bacteriology · 2025Review
- Structural basis for allosteric modulation of M. tuberculosis proteasome core particle.Nature communications · 2025Article
- Substrates bind to residues lining the ring of asymmetrically engaged bacterial proteasome activator Bpa.Nature communications · 2025Article
- ATP-independent substrate recruitment to proteasomal degradation in mycobacteria.Life science alliance · 2023Article
- Article
- Structural determinants of regulated proteolysis in pathogenic bacteria by ClpP and the proteasome.Current opinion in structural biology · 2021Review
- Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Control of Toxin-Antitoxin Systems by Proteases inFrontiers in molecular biosciences · 2021Review
- Survival in Hostile Conditions: Pupylation and the Proteasome in Actinobacterial Stress Response Pathways.Frontiers in molecular biosciences · 2021Review
- Psoralen Derivatives as Inhibitors ofMolecules (Basel, Switzerland) · 2020Article
- Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis.Scientific reports · 2019Article
- Biology and Biochemistry of Bacterial Proteasomes.Sub-cellular biochemistry · 2019Review
- The Bacterial Proteasome at the Core of Diverse Degradation Pathways.Frontiers in molecular biosciences · 2019Review
- Article
- Targeting the Proteostasis Network for Mycobacterial Drug Discovery.ACS infectious diseases · 2018Review
- Proteasome substrate capture and gate opening by the accessory factor PafE fromThe Journal of biological chemistry · 2018Article
- Mycobacterium tuberculosis proteasomal ATPase Mpa has a β-grasp domain that hinders docking with the proteasome core protease.Molecular microbiology · 2017Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The occurrence of the proteasome in bacteria is limited to the phylum of actinobacteria, where it is maintained in parallel to the usual bacterial compartmentalizing proteases. The role it plays in these organisms is still not fully understood, but in the human pathogen Mycobacterium tuberculosis (Mtb) the proteasome supports persistence in the host. In complex with the ring-shaped ATPase Mpa (called ARC in other actinobacteria), the proteasome can degrade proteins that have been post-translationally modified with the prokaryotic ubiquitin-like protein Pup. Unlike for the eukaryotic proteasome core particle, no other bacterial proteasome interactors have been identified to date. Here we describe and characterize a novel bacterial proteasome activator of Mycobacterium tuberculosis we termed Bpa (Rv3780), using a combination of biochemical and biophysical methods. Bpa features a canonical C-terminal proteasome interaction motif referred to as the HbYX motif, and its orthologs are only found in those actinobacteria encoding the proteasomal subunits. Bpa can inhibit degradation of Pup-tagged substrates in vitro by competing with Mpa for association with the proteasome. Using negative-stain electron microscopy, we show that Bpa forms a ring-shaped homooligomer that can bind coaxially to the face of the proteasome cylinder. Interestingly, Bpa can stimulate the proteasomal degradation of the model substrate β-casein, which suggests it could play a role in the removal of non-native or damaged proteins.
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