ReviewFrontiers in molecular biosciences2019
The Bacterial Proteasome at the Core of Diverse Degradation Pathways.
Review in Frontiers in molecular biosciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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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
19 citing papers in PubMed, 36 citations in OpenAlex.
- Association Between the Root Canal Microbiome and Apical Lesion Size: An Observational Shotgun Metagenomic Study.International endodontic journal · 2026Observational
- Cleaving Expectations: A Review of Proteasome Functional and Catalytic Diversity.Biomolecules · 2025Review
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- Bimodular architecture of bacterial effector SAP05 that drives ubiquitin-independent targeted protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Novel WYL domain-containing transcriptional activator acts in response to genotoxic stress in rapidly growing mycobacteria.Communications biology · 2023Article
- Degradation Mechanism of AAA+ Proteases and Regulation ofBiomolecules · 2022Review
- Phosphoproteome Dynamics of Streptomyces rimosus during Submerged Growth and Antibiotic Production.mSystems · 2022Article
- The novel genus, 'Candidatus Phosphoribacter', previously identified as Tetrasphaera, is the dominant polyphosphate accumulating lineage in EBPR wastewater treatment plants worldwide.The ISME journal · 2022Article
- Article
- Structural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex.Nature communications · 2022Article
- Protein degradation control and regulation of bacterial survival and pathogenicity: the role of protein degradation systems in bacteria.Molecular biology reports · 2021Review
- Article
- 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
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Protective Roles of Cytosolic and Plastidal Proteasomes on Abiotic Stress and Pathogen Invasion.Plants (Basel, Switzerland) · 2020Review
- Modification of the host ubiquitome by bacterial enzymes.Microbiological research · 2020Review
- AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms.Biomolecules · 2020Review
- Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis.Scientific reports · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteasomal protein degradation exists in mycobacteria and other actinobacteria, and expands their repertoire of compartmentalizing protein degradation pathways beyond the usual bacterial types. A product of horizontal gene transfer, bacterial proteasomes have evolved to support the organism's survival under challenging environmental conditions like nutrient starvation and physical or chemical stresses. Like the eukaryotic 20S proteasome, the bacterial core particle is gated and must associate with a regulator complex to form a fully active protease capable of recruiting and internalizing substrate proteins. By association with diverse regulator complexes that employ different recruitment strategies, the bacterial 20S core particle is able to act in different cellular degradation pathways. In association with the mycobacterial proteasomal ATPase Mpa, the proteasome degrades substrates post-translationally modified with prokaryotic, ubiquitin-like protein Pup in a process called pupylation. Upon interaction with the ATP-independent bacterial proteasome activator Bpa, poorly structured substrates are recruited for proteasomal degradation. A potential third degradation route might employ a Cdc48-like protein of actinobacteria (Cpa), for which interaction with the 20S core was recently demonstrated but no degradation substrates have been identified yet. The alternative interaction partners and wide range of substrate proteins suggest that the bacterial proteasome is a modular, functionally flexible and conditionally regulated degradation machine in bacteria that encounter rapidly changing and challenging conditions.
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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.