ArticleJournal of bacteriology2012
The PduM protein is a structural component of the microcompartments involved in coenzyme B(12)-dependent 1,2-propanediol degradation by Salmonella enterica.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 69 citations in OpenAlex.
- The Dark Side of Green Energy: Glycol Waste and the Microbes That Can Transform It.Molecules (Basel, Switzerland) · 2026Review
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- Heterologous Assembly of Pleomorphic Bacterial Microcompartment Shell Architectures Spanning the Nano- to Microscale.Advanced materials (Deerfield Beach, Fla.) · 2023Article
- A method for targeting a specified segment of DNA to a bacterial microorganelle.Nucleic acids research · 2022Article
- Linking the Salmonella enterica 1,2-Propanediol Utilization Bacterial Microcompartment Shell to the Enzymatic Core via the Shell Protein PduB.Journal of bacteriology · 2022Article
- Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology.Nature communications · 2022Article
- Biogenesis of a bacterial metabolosome for propanediol utilization.Nature communications · 2022Article
- Chemical probing provides insight into the native assembly state of a bacterial microcompartment.Structure (London, England : 1993) · 2022Article
- Symmetry breaking and structural polymorphism in a bacterial microcompartment shell protein for choline utilization.Protein science : a publication of the Protein Society · 2020Article
- Prokaryotic Organelles: Bacterial Microcompartments inEcoSal Plus · 2020Review
- Decoding the stoichiometric composition and organisation of bacterial metabolosomes.Nature communications · 2020Article
- Article
- Exploring Bacterial Microcompartments in the Acetogenic BacteriumFrontiers in microbiology · 2020Article
- Engineering the PduT shell protein to modify the permeability of the 1,2-propanediol microcompartment ofMicrobiology (Reading, England) · 2019Article
- Deep-Subsurface Pressure Stimulates Metabolic Plasticity in Shale-ColonizingApplied and environmental microbiology · 2019Article
- Inflammation associated ethanolamine facilitates infection by Crohn's disease-linked adherent-invasive Escherichia coli.EBioMedicine · 2019Article
- Bacterial Microcompartment-Dependent 1,2-Propanediol Utilization Stimulates Anaerobic Growth ofFrontiers in microbiology · 2019Article
- Cargo encapsulation in bacterial microcompartments: Methods and analysis.Methods in enzymology · 2019Article
- Transfer and analysis of Salmonella pdu genes in a range of Gram-negative bacteria demonstrate exogenous microcompartment expression across a variety of species.Microbial biotechnology · 2018Article
- Re-directing bacterial microcompartment systems to enhance recombinant expression of lysis protein E from bacteriophage ϕX174 in Escherichia coli.Microbial cell factories · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Diverse bacteria use proteinaceous microcompartments (MCPs) to optimize metabolic pathways that have toxic or volatile intermediates. MCPs consist of metabolic enzymes encased within a protein shell that provides a defined environment. In Salmonella enterica, a MCP is involved in B(12)-dependent 1,2-propanediol utilization (Pdu MCP). In this report, we show that the protein PduM is required for the assembly and function of the Pdu MCP. The results of tandem mass spectrometry and Western blot analyses show that PduM is a component of the Pdu MCP. Electron microscopy shows that a pduM deletion mutant forms MCPs with abnormal morphology. Growth tests and metabolite measurements establish that a pduM deletion mutant is unable to form functional MCPs. PduM is unrelated in sequence to proteins of known function and hence may represent a new class of MCP structural proteins. We also report a modified protocol for the purification of Pdu MCP from Salmonella which allows isolation of milligram amounts of MCPs in about 4 h. We believe that this protocol can be extended or modified for the purification of MCPs from diverse bacteria.
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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.