ArticleProceedings of the National Academy of Sciences of the United States of America2015
An adenosine triphosphate-independent proteasome activator contributes to the virulence of Mycobacterium tuberculosis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 47 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
- ClpC1-targeting peptide natural products differentially dysregulate the proteome of Mycobacterium tuberculosis.Nature communications · 2026Article
- "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
- Aldehyde accumulation inmBio · 2023Article
- Article
- Structural determinants of regulated proteolysis in pathogenic bacteria by ClpP and the proteasome.Current opinion in structural biology · 2021Review
- The Pup-Proteasome System Protects Mycobacteria from Antimicrobial Antifolates.Antimicrobial agents and chemotherapy · 2021Article
- 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
- Article
- Selective Phenylimidazole-Based Inhibitors of theJournal of medicinal chemistry · 2019Article
- Characterization of Guided Entry of Tail-Anchored Proteins 3 Homologues in Mycobacterium tuberculosis.Journal of bacteriology · 2019Article
- Biology and Biochemistry of Bacterial Proteasomes.Sub-cellular biochemistry · 2019Review
- Highlighting the Proteasome: Using Fluorescence to Visualize Proteasome Activity and Distribution.Frontiers in molecular biosciences · 2019Review
- The Bacterial Proteasome at the Core of Diverse Degradation Pathways.Frontiers in molecular biosciences · 2019Review
- Article
Corrections and comments
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Authors and funding
12 authors at 7 institutions in 2 countries.
Funding
Abstract
Mycobacterium tuberculosis encodes a proteasome that is highly similar to eukaryotic proteasomes and is required to cause lethal infections in animals. The only pathway known to target proteins for proteasomal degradation in bacteria is pupylation, which is functionally analogous to eukaryotic ubiquitylation. However, evidence suggests that the M. tuberculosis proteasome contributes to pupylation-independent pathways as well. To identify new proteasome cofactors that might contribute to such pathways, we isolated proteins that bound to proteasomes overproduced in M. tuberculosis and found a previously uncharacterized protein, Rv3780, which formed rings and capped M. tuberculosis proteasome core particles. Rv3780 enhanced peptide and protein degradation by proteasomes in an adenosine triphosphate (ATP)-independent manner. We identified putative Rv3780-dependent proteasome substrates and found that Rv3780 promoted robust degradation of the heat shock protein repressor, HspR. Importantly, an M. tuberculosis Rv3780 mutant had a general growth defect, was sensitive to heat stress, and was attenuated for growth in mice. Collectively, these data demonstrate that ATP-independent proteasome activators are not confined to eukaryotes and can contribute to the virulence of one the world's most devastating pathogens.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.