ArticleThe Journal of biological chemistry2015
Localization of proteins to the 1,2-propanediol utilization microcompartment by non-native signal sequences is mediated by a common hydrophobic motif.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Article
- Article
- Engineering COPlant communications · 2025Article
- Bacterial microcompartments as a next-generation metabolic engineering tool: utilizing nature's solution for confining challenging catabolic pathways.Biochemical Society transactions · 2024Review
- Microbial Fermentation of Polyethylene Terephthalate (PET) Plastic Waste for the Production of Chemicals or Electricity.Angewandte Chemie (International ed. in English) · 2022Article
- Localization and interaction studies of the Salmonella enterica ethanolamine ammonia-lyase (EutBC), its reactivase (EutA), and the EutT corrinoid adenosyltransferase.Molecular microbiology · 2022Article
- Chemical probing provides insight into the native assembly state of a bacterial microcompartment.Structure (London, England : 1993) · 2022Article
- Complex structure reveals CcmM and CcmN form a heterotrimeric adaptor in β-carboxysome.Protein science : a publication of the Protein Society · 2021Article
- Engineering spatiotemporal organization and dynamics in synthetic cells.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2021Review
- Prokaryotic Organelles: Bacterial Microcompartments inEcoSal Plus · 2020Review
- Engineered bacterial microcompartments: apps for programming metabolism.Current opinion in biotechnology · 2020Review
- Enzyme Assembly for Compartmentalized Metabolic Flux Control.Metabolites · 2020Review
- Article
- Engineering the PduT shell protein to modify the permeability of the 1,2-propanediol microcompartment ofMicrobiology (Reading, England) · 2019Article
- A designed bacterial microcompartment shell with tunable composition and precision cargo loading.Metabolic engineering · 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
- Deciphering molecular details in the assembly of alpha-type carboxysome.Scientific reports · 2018Article
- An estimate is worth about a thousand experiments: using order-of-magnitude estimates to identify cellular engineering targets.Microbial cell factories · 2018Review
- De novo targeting to the cytoplasmic and luminal side of bacterial microcompartments.Nature communications · 2018Article
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5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Various bacteria localize metabolic pathways to proteinaceous organelles known as bacterial microcompartments (MCPs), enabling the metabolism of carbon sources to enhance survival and pathogenicity in the gut. There is considerable interest in exploiting bacterial MCPs for metabolic engineering applications, but little is known about the interactions between MCP signal sequences and the protein shells of different MCP systems. We found that the N-terminal sequences from the ethanolamine utilization (Eut) and glycyl radical-generating protein MCPs are able to target reporter proteins to the 1,2-propanediol utilization (Pdu) MCP, and that this localization is mediated by a conserved hydrophobic residue motif. Recapitulation of this motif by the addition of a single amino acid conferred targeting function on an N-terminal sequence from the ethanol utilization MCP system that previously did not act as a Pdu signal sequence. Moreover, the Pdu-localized signal sequences competed with native Pdu targeting sequences for encapsulation in the Pdu MCP. Salmonella enterica natively possesses both the Pdu and Eut operons, and our results suggest that Eut proteins might be localized to the Pdu MCP in vivo. We further demonstrate that S. enterica LT2 retained the ability to grow on 1,2-propanediol as the sole carbon source when a Pdu enzyme was replaced with its Eut homolog. Although the relevance of this finding to the native system remains to be explored, we show that the Pdu-localized signal sequences described herein allow control over the ratio of heterologous proteins encapsulated within Pdu MCPs.
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