ArticleProceedings of the National Academy of Sciences of the United States of America2016
The pupylation machinery is involved in iron homeostasis by targeting the iron storage protein ferritin.
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. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 45 citations in OpenAlex.
- The terminal heme synthetic enzyme, coproheme decarboxylase, negatively regulates heme uptake in Mycobacterium tuberculosis.The Journal of biological chemistry · 2026Article
- "Pupdates" on proteasomal degradation in bacteria.Journal of bacteriology · 2025Review
- Identification of a depupylation regulator for an essential enzyme inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Functional analysis of the whole CYPome and Fdxome ofEngineering microbiology · 2024Article
- Regulation of heme biosynthesis via the coproporphyrin dependent pathway in bacteria.Frontiers in microbiology · 2024Review
- Improving growth properties of Corynebacterium glutamicum by implementing an iron-responsive protocatechuate biosynthesis.Microbial biotechnology · 2023Article
- Degradation Mechanism of AAA+ Proteases and Regulation ofBiomolecules · 2022Review
- Transcriptomic Analysis of the Dual Response of Rhodococcus aetherivorans BCP1 to Inorganic Arsenic Oxyanions.Applied and environmental microbiology · 2022Article
- A novel strategy of gene screen based on multi-omics in Streptomyces roseosporus.Applied microbiology and biotechnology · 2022Article
- Structural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex.Nature communications · 2022Article
- Berberine alleviates liver fibrosis through inducing ferrous redox to activate ROS-mediated hepatic stellate cells ferroptosis.Cell death discovery · 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 iron chelator, PBT434, modulates transcellular iron trafficking in brain microvascular endothelial cells.PloS one · 2021Article
- The Iron Deficiency Response of Corynebacterium glutamicum and a Link to Thiamine Biosynthesis.Applied and environmental microbiology · 2020Article
- COmBio · 2020Article
- Protein post-translational modifications in bacteria.Nature reviews. Microbiology · 2019Review
- Development of a novel, robust and cost-efficient process for valorizing dairy waste exemplified by ethanol production.Microbial cell factories · 2019Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Impact of Autophagy and Aging on Iron Load and Ferritin inFrontiers in cell and developmental biology · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The balance of sufficient iron supply and avoidance of iron toxicity by iron homeostasis is a prerequisite for cellular metabolism and growth. Here we provide evidence that, in Actinobacteria, pupylation plays a crucial role in this process. Pupylation is a posttranslational modification in which the prokaryotic ubiquitin-like protein Pup is covalently attached to a lysine residue in target proteins, thus resembling ubiquitination in eukaryotes. Pupylated proteins are recognized and unfolded by a dedicated AAA+ ATPase (Mycobacterium proteasomal AAA+ ATPase; ATPase forming ring-shaped complexes). In Mycobacteria, degradation of pupylated proteins by the proteasome serves as a protection mechanism against several stress conditions. Other bacterial genera capable of pupylation such as Corynebacterium lack a proteasome, and the fate of pupylated proteins is unknown. We discovered that Corynebacterium glutamicum mutants lacking components of the pupylation machinery show a strong growth defect under iron limitation, which was caused by the absence of pupylation and unfolding of the iron storage protein ferritin. Genetic and biochemical data support a model in which the pupylation machinery is responsible for iron release from ferritin independent of degradation.
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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.