ArticleNature chemical biology2018
Engineered synthetic scaffolds for organizing proteins within the bacterial cytoplasm.
Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
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Who cites it
60 citing papers in PubMed, 152 citations in OpenAlex.
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- A Paradigm Shift in Microbial Protein Manufacturing.Life (Basel, Switzerland) · 2026Review
- Microcompartments in archaeal ancestors of eukaryotes: a bioenergetic engine that could have fuelled eukaryogenesis.bioRxiv : the preprint server for biology · 2025Article
- Mutation-induced filaments of folded proteins are inert and non-toxic in a cellular system.Molecular systems biology · 2025Article
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- De novo biosynthesis of nylon 12 monomer ω-aminododecanoic acid.Nature communications · 2025Article
- The art of designed coiled-coils for the regulation of mammalian cells.Cell chemical biology · 2024Review
- Maturation and Conformational Switching of aJournal of the American Chemical Society · 2024Article
- Nanoengineering Carboxysome Shells for Protein Cages with Programmable Cargo Targeting.ACS nano · 2024Article
- Construction of an engineeredSynthetic and systems biotechnology · 2024Article
- Assembling membraneless organelles from de novo designed proteins.Nature chemistry · 2024Article
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- Design and Selection of Heterodimerizing Helical Hairpins for Synthetic Biology.ACS synthetic biology · 2023Article
- Rational Design of Phosphorylation-Responsive Coiled Coil-Peptide Assemblies.ACS synthetic biology · 2023Article
- Engineering synthetic biomolecular condensates.Nature reviews bioengineering · 2023Review
- Synthetic biology promotes the capture of CO2 to produce fatty acid derivatives in microbial cell factories.Bioresources and bioprocessing · 2022Review
- Metabolic pathway assembly using docking domains from type I cis-AT polyketide synthases.Nature communications · 2022Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
We have developed a system for producing a supramolecular scaffold that permeates the entire Escherichia coli cytoplasm. This cytoscaffold is constructed from a three-component system comprising a bacterial microcompartment shell protein and two complementary de novo coiled-coil peptides. We show that other proteins can be targeted to this intracellular filamentous arrangement. Specifically, the enzymes pyruvate decarboxylase and alcohol dehydrogenase have been directed to the filaments, leading to enhanced ethanol production in these engineered bacterial cells compared to those that do not produce the scaffold. This is consistent with improved metabolic efficiency through enzyme colocation. Finally, the shell-protein scaffold can be directed to the inner membrane of the cell, demonstrating how synthetic cellular organization can be coupled with spatial optimization through in-cell protein design. The cytoscaffold has potential in the development of next-generation cell factories, wherein it could be used to organize enzyme pathways and metabolite transporters to enhance metabolic flux.
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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.