ArticlePLoS pathogens2010
The Mycobacterium tuberculosis proteasome active site threonine is essential for persistence yet dispensable for replication and resistance to nitric oxide.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 89 citations in OpenAlex.
- The phage shock protein A (PspA) maintains membrane potential and supports NADH dehydrogenase function in mycobacteria.bioRxiv : the preprint server for biology · 2026Article
- Fred Goldberg machines in the pathogenesis of Mycobacterium tuberculosis.The Journal of biological chemistry · 2026Review
- A Key Metabolic Protein in Active Mycobacterium tuberculosis: Insights into Carbon, Nitrogen, and Sulfur Metabolism.Advances in experimental medicine and biology · 2026Review
- Gene Regulatory Mechanism of Mycobacterium Tuberculosis during Dormancy.Current issues in molecular biology · 2024Review
- Comprehensive essentiality analysis of themBio · 2023Article
- OvercomingActa pharmaceutica Sinica. B · 2022Review
- Genome-Wide Study of Drug ResistantMicroorganisms · 2022Article
- Microbial proteasomes as drug targets.PLoS pathogens · 2021Review
- Insights into the molecular determinants involved inVirulence · 2021Review
- Macrocyclic Peptides that Selectively Inhibit theJournal of medicinal chemistry · 2021Article
- The Pup-Proteasome System Protects Mycobacteria from Antimicrobial Antifolates.Antimicrobial agents and chemotherapy · 2021Article
- Nonredundant functions of Mycobacterium tuberculosis chaperones promote survival under stress.Molecular microbiology · 2021Article
- Selective Phenylimidazole-Based Inhibitors of theJournal of medicinal chemistry · 2019Article
- Phenolic Compounds as Promising Drug Candidates in Tuberculosis Therapy.Molecules (Basel, Switzerland) · 2019Review
- Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation.PloS one · 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
- Ubiquitin, SUMO, and NEDD8: Key Targets of Bacterial Pathogens.Trends in cell biology · 2018Review
- Article
- Targeting the Proteostasis Network for Mycobacterial Drug Discovery.ACS infectious diseases · 2018Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Previous work revealed that conditional depletion of the core proteasome subunits PrcB and PrcA impaired growth of Mycobacterium tuberculosis in vitro and in mouse lungs, caused hypersusceptibility to nitric oxide (NO) and impaired persistence of the bacilli during chronic mouse infections. Here, we show that genetic deletion of prcBA led to similar phenotypes. Surprisingly, however, an active site mutant proteasome complemented the in vitro and in vivo growth defects of the prcBA knockout (Delta prcBA) as well as its NO hypersensitivity. In contrast, long-term survival of M. tuberculosis in stationary phase and during starvation in vitro and in the chronic phase of mouse infection required a proteolytically active proteasome. Inhibition of inducible nitric oxide synthase did not rescue survival of Delta prcBA, revealing a function beyond NO defense, by which the proteasome contributes to M. tuberculosis fitness during chronic mouse infections. These findings suggest that proteasomal proteolysis facilitates mycobacterial persistence, that M. tuberculosis faces starvation during chronic mouse infections and that the proteasome serves a proteolysis-independent function.
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Registered trials
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