ArticleThe EMBO journal2014
Survival of mycobacteria depends on proteasome-mediated amino acid recycling under nutrient limitation.
Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed, 87 citations in OpenAlex.
- A Key Metabolic Protein in Active Mycobacterium tuberculosis: Insights into Carbon, Nitrogen, and Sulfur Metabolism.Advances in experimental medicine and biology · 2026Review
- "Pupdates" on proteasomal degradation in bacteria.Journal of bacteriology · 2025Review
- Structural basis for allosteric modulation of M. tuberculosis proteasome core particle.Nature communications · 2025Article
- The Asgard archaeal ESCRT-III system forms helical filaments and remodels eukaryotic-like membranes.The EMBO journal · 2025Article
- BCG-derived acellular membrane vesicles elicit antimycobacterial immunity and innate immune memory.Frontiers in immunology · 2025Article
- Identification of a depupylation regulator for an essential enzyme inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Turnover of the extracellular polymeric matrix of granules performing biological phosphate removal.Applied microbiology and biotechnology · 2023Article
- Structural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex.Nature communications · 2022Article
- Article
- Exploring Protein Space: From Hydrolase to Ligase by Substitution.Molecular biology and evolution · 2021Article
- Survival in Hostile Conditions: Pupylation and the Proteasome in Actinobacterial Stress Response Pathways.Frontiers in molecular biosciences · 2021Review
- Control of Toxin-Antitoxin Systems by Proteases inFrontiers in molecular biosciences · 2021Review
- The genetic proteome: Using genetics to inform the proteome of mycobacterial pathogens.PLoS pathogens · 2021Review
- Active metabolism unmasks functional protein-protein interactions in real time in-cell NMR.Communications biology · 2020Article
- Protein post-translational modifications in bacteria.Nature reviews. Microbiology · 2019Review
- TheProceedings of the National Academy of Sciences of the United States of America · 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
- Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation.PloS one · 2019Article
- Defining the Transcriptional and Post-transcriptional Landscapes ofFrontiers in microbiology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intracellular protein degradation is an essential process in all life domains. While in all eukaryotes regulated protein degradation involves ubiquitin tagging and the 26S-proteasome, bacterial prokaryotic ubiquitin-like protein (Pup) tagging and proteasomes are conserved only in species belonging to the phyla Actinobacteria and Nitrospira. In Mycobacterium tuberculosis, the Pup-proteasome system (PPS) is important for virulence, yet its physiological role in non-pathogenic species has remained an enigma. We now report, using Mycobacterium smegmatis as a model organism, that the PPS is essential for survival under starvation. Upon nitrogen limitation, PPS activity is induced, leading to accelerated tagging and degradation of many cytoplasmic proteins. We suggest a model in which the PPS functions to recycle amino acids under nitrogen starvation, thereby enabling the cell to maintain basal metabolic activities. We also find that the PPS auto-regulates its own activity via pupylation and degradation of its components in a manner that promotes the oscillatory expression of PPS components. As such, the destructive activity of the PPS is carefully balanced to maintain cellular functions during starvation.
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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.