ArticleProceedings of the National Academy of Sciences of the United States of America2012
Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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
63 citing papers in PubMed, 133 citations in OpenAlex.
- Employing Nanotechnology to Enhance Ethanol Production in Two Synechococcus elongatus Strains.Chembiochem : a European journal of chemical biology · 2026Article
- Engineering New-to-Nature Biological Pathways for β,γ-Alkanediol Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- A blueprint for biomolecular condensation driven by bacterial microcompartment encapsulation peptides.Nature communications · 2025Article
- A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Article
- Nanoengineering Carboxysome Shells for Protein Cages with Programmable Cargo Targeting.ACS nano · 2024Article
- Modeling bacterial microcompartment architectures for enhanced cyanobacterial carbon fixation.Frontiers in plant science · 2024Review
- Article
- Modification of bacterial microcompartments with target biomoleculesMaterials advances · 2023Article
- Linking the Salmonella enterica 1,2-Propanediol Utilization Bacterial Microcompartment Shell to the Enzymatic Core via the Shell Protein PduB.Journal of bacteriology · 2022Article
- Chemical probing provides insight into the native assembly state of a bacterial microcompartment.Structure (London, England : 1993) · 2022Article
- Variety of size and form of GRM2 bacterial microcompartment particles.Protein science : a publication of the Protein Society · 2021Article
- Advances in the World of Bacterial Microcompartments.Trends in biochemical sciences · 2021Review
- Article
- Prokaryotic Organelles: Bacterial Microcompartments inEcoSal Plus · 2020Review
- Effect of metabolosome encapsulation peptides on enzyme activity, coaggregation, incorporation, and bacterial microcompartment formation.MicrobiologyOpen · 2020Article
- Decoding the stoichiometric composition and organisation of bacterial metabolosomes.Nature communications · 2020Article
- Enzyme Assembly for Compartmentalized Metabolic Flux Control.Metabolites · 2020Review
- Encapsulation mechanisms and structural studies of GRM2 bacterial microcompartment particles.Nature communications · 2020Article
- Engineering the PduT shell protein to modify the permeability of the 1,2-propanediol microcompartment ofMicrobiology (Reading, England) · 2019Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial microcompartments (MCPs) are a widespread family of proteinaceous organelles that consist of metabolic enzymes encapsulated within a protein shell. For MCPs to function specific enzymes must be encapsulated. We recently reported that a short N-terminal targeting sequence of propionaldehyde dehydrogenase (PduP) is necessary and sufficient for the packaging of enzymes into a MCP that functions in 1,2-propanediol (1,2-PD) utilization (Pdu) by Salmonella enterica. Here we show that encapsulation is mediated by binding of the PduP targeting sequence to a short C-terminal helix of the PduA shell protein. In vitro studies indicated binding between PduP and PduA (and PduJ) but not other MCP shell proteins. Alanine scanning mutagenesis determined that the key residues involved in binding are E7, I10, and L14 of PduP and H81, V84, and L88 of PduA. In vivo targeting studies indicated that the binding between the N terminus of PduP and the C terminus of PduA is critical for encapsulation of PduP within the Pdu MCP. Structural models suggest that the N terminus of PduP and C terminus of PduA both form helical structures that bind one another via the key residues identified by mutagenesis. Cumulatively, these results show that the N-terminal targeting sequence of PduP promotes its encapsulation by binding to MCP shell proteins. This is a unique report determining the mechanism by which a MCP targeting sequence functions. We propose that specific interactions between the termini of shell proteins and lumen enzymes have general importance for guiding the assembly and the higher level organization of bacterial MCPs.
Indexed as
Identifiers
What OpenQuestion holds
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.