ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structural analysis of the dodecameric proteasome activator PafE in Mycobacterium tuberculosis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 28 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
- "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
- Proteasome Activators and Ageing: Restoring Proteostasis Using Small Molecules.Sub-cellular biochemistry · 2024Review
- ATP-independent substrate recruitment to proteasomal degradation in mycobacteria.Life science alliance · 2023Article
- Article
- Microbial proteasomes as drug targets.PLoS pathogens · 2021Review
- Macrocyclic Peptides that Selectively Inhibit theJournal of medicinal chemistry · 2021Article
- Allosteric coupling between α-rings of the 20S proteasome.Nature communications · 2020Article
- Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis.Scientific reports · 2019Article
- Selective Phenylimidazole-Based Inhibitors of theJournal of medicinal chemistry · 2019Article
- The Bacterial Proteasome at the Core of Diverse Degradation Pathways.Frontiers in molecular biosciences · 2019Review
- Biology and Biochemistry of Bacterial Proteasomes.Sub-cellular biochemistry · 2019Review
- 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
- Structural Analysis of Mycobacterium tuberculosis Homologues of the Eukaryotic Proteasome Assembly Chaperone 2 (PAC2).Journal of bacteriology · 2017Article
- Loss-of-Function Mutations in HspR Rescue the Growth Defect of a Mycobacterium tuberculosis Proteasome Accessory Factor E (Journal of bacteriology · 2017Article
- Bacterial Proteasomes: Mechanistic and Functional Insights.Microbiology and molecular biology reviews : MMBR · 2017Review
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The human pathogen Mycobacterium tuberculosis (Mtb) requires a proteasome system to cause lethal infections in mice. We recently found that proteasome accessory factor E (PafE, Rv3780) activates proteolysis by the Mtb proteasome independently of adenosine triphosphate (ATP). Moreover, PafE contributes to the heat-shock response and virulence of Mtb Here, we show that PafE subunits formed four-helix bundles similar to those of the eukaryotic ATP-independent proteasome activator subunits of PA26 and PA28. However, unlike any other known proteasome activator, PafE formed dodecamers with 12-fold symmetry, which required a glycine-XXX-glycine-XXX-glycine motif that is not found in previously described activators. Intriguingly, the truncation of the PafE carboxyl-terminus resulted in the robust binding of PafE rings to native proteasome core particles and substantially increased proteasomal activity, suggesting that the extended carboxyl-terminus of this cofactor confers suboptimal binding to the proteasome core particle. Collectively, our data show that proteasomal activation is not limited to hexameric ATPases in bacteria.
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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.