ArticleeLife2022
Cellular assays identify barriers impeding iron-sulfur enzyme activity in a non-native prokaryotic host.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Discovery of an Antiviral Electron Transfer Process to Create Catalytically Self-Sufficient Viral Restriction Factors.Angewandte Chemie (International ed. in English) · 2026Article
- Heterologous iron-sulfur cluster biogenesis and delivery for cytosolic isobutanol and isopentanol production inbioRxiv : the preprint server for biology · 2026Article
- Functional analysis of the methylerythritol phosphate pathway terminal enzymes IspG and IspH fromMicrobiology spectrum · 2024Article
- Discovery of a Biotin Synthase That Utilizes an Auxiliary 4Fe-5S Cluster for Sulfur Insertion.Journal of the American Chemical Society · 2024Article
- Cytosolic iron-sulfur protein assembly system identifies clients by a C-terminal tripeptide.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Maturation strategy influences expression levels and cofactor occupancy in Fe-S proteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
Corrections and comments
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Authors and funding
18 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Iron-sulfur (Fe-S) clusters are ancient and ubiquitous protein cofactors and play irreplaceable roles in many metabolic and regulatory processes. Fe-S clusters are built and distributed to Fe-S enzymes by dedicated protein networks. The core components of these networks are widely conserved and highly versatile. However, Fe-S proteins and enzymes are often inactive outside their native host species. We sought to systematically investigate the compatibility of Fe-S networks with non-native Fe-S enzymes. By using collections of Fe-S enzyme orthologs representative of the entire range of prokaryotic diversity, we uncovered a striking correlation between phylogenetic distance and probability of functional expression. Moreover, coexpression of a heterologous Fe-S biogenesis pathway increases the phylogenetic range of orthologs that can be supported by the foreign host. We also find that Fe-S enzymes that require specific electron carrier proteins are rarely functionally expressed unless their taxon-specific reducing partners are identified and co-expressed. We demonstrate how these principles can be applied to improve the activity of a radical
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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.