ArticleJournal of bacteriology2017
The N Terminus of the PduB Protein Binds the Protein Shell of the Pdu Microcompartment to Its Enzymatic Core.
Article in Journal of bacteriology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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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.
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Who cites it
22 citing papers in PubMed, 58 citations in OpenAlex.
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- Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.Journal of virology · 2026Review
- Assembly and Functional Coordination of Two Families of Metabolic Organelles in Salmonella.Microbial biotechnology · 2026Article
- Biological semiconductors: self-assembled shell proteins as photoactive materials.Chemical science · 2026Article
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- Modeling bacterial microcompartment architectures for enhanced cyanobacterial carbon fixation.Frontiers in plant science · 2024Review
- Linking the Salmonella enterica 1,2-Propanediol Utilization Bacterial Microcompartment Shell to the Enzymatic Core via the Shell Protein PduB.Journal of bacteriology · 2022Article
- Getting the Payload in Place - Unravelling the Complexities of Making a Bacterial Microcompartment.Journal of bacteriology · 2022Article
- Microcompartment assembly around multicomponent fluid cargoes.The Journal of chemical physics · 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
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- Isolation of a member of the candidate phylum 'Atribacteria' reveals a unique cell membrane structure.Nature communications · 2020Article
- Prokaryotic Organelles: Bacterial Microcompartments inEcoSal Plus · 2020Review
- Decoding the stoichiometric composition and organisation of bacterial metabolosomes.Nature communications · 2020Article
- Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles.Nature communications · 2020Article
- Exploring Bacterial Microcompartments in the Acetogenic BacteriumFrontiers in microbiology · 2020Article
- Article
- Engineering the PduT shell protein to modify the permeability of the 1,2-propanediol microcompartment ofMicrobiology (Reading, England) · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial microcompartments (MCPs) are extremely large proteinaceous organelles that consist of an enzymatic core encapsulated within a complex protein shell. A key question in MCP biology is the nature of the interactions that guide the assembly of thousands of protein subunits into a well-ordered metabolic compartment. In this report, we show that the N-terminal 37 amino acids of the PduB protein have a critical role in binding the shell of the 1,2-propanediol utilization (Pdu) microcompartment to its enzymatic core. Several mutations were constructed that deleted short regions of the N terminus of PduB. Growth tests indicated that three of these deletions were impaired MCP assembly. Attempts to purify MCPs from these mutants, followed by gel electrophoresis and enzyme assays, indicated that the protein complexes isolated consisted of MCP shells depleted of core enzymes. Electron microscopy substantiated these findings by identifying apparently empty MCP shells but not intact MCPs. Analyses of 13 site-directed mutants indicated that the key region of the N terminus of PduB required for MCP assembly is a putative helix spanning residues 6 to 18. Considering the findings presented here together with prior work, we propose a new model for MCP assembly.
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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.