ArticleProceedings of the National Academy of Sciences of the United States of America2015
A distinct pathway for tetrahymanol synthesis in bacteria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 82 citations in OpenAlex.
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- Single-cell transcriptomics reveals lateral transfers of multiple functional genes from prokaryotes to free-living ciliated protists in detrital food webs.Marine life science & technology · 2026Article
- Orthogonal chemical genomics approaches reveal genomic targets for increasing anaerobic chemical tolerance inmSystems · 2026Article
- The Evolutionary History and Modern Diversity of Triterpenoid Cyclases.Molecular biology and evolution · 2025Article
- The evolutionary history and modern diversity of triterpenoid cyclases.bioRxiv : the preprint server for biology · 2025Article
- Methane fueled lake pelagic food webs in a Cretaceous greenhouse world.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Hopanoid lipids promote soybeanmBio · 2024Article
- Lipid biomarkers: molecular tools for illuminating the history of microbial life.Nature reviews. Microbiology · 2022Review
- Identification and a phased pH control strategy of diosgenin bio-synthesized by an endogenous Bacillus licheniformis Syt1 derived from Dioscorea zingiberensis C. H. Wright.Applied microbiology and biotechnology · 2021Article
- A squalene-hopene cyclase inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Variation of salinity and nitrogen concentration affects the pentacyclic triterpenoid inventory of the haloalkaliphilic aerobic methanotrophic bacterium Methylotuvimicrobium alcaliphilum.Extremophiles : life under extreme conditions · 2021Article
- Concerning P450 Evolution: Structural Analyses Support Bacterial Origin of Sterol 14α-Demethylases.Molecular biology and evolution · 2021Article
- Phytosterol Profiles, Genomes and Enzymes - An Overview.Frontiers in plant science · 2021Review
- Microbial biomarkers reveal a hydrothermally active landscape at Olduvai Gorge at the dawn of the Acheulean, 1.7 Ma.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Squalene-Tetrahymanol Cyclase Expression Enables Sterol-Independent Growth of Saccharomyces cerevisiae.Applied and environmental microbiology · 2020Article
- Review
- Hopanoid lipids: from membranes to plant-bacteria interactions.Nature reviews. Microbiology · 2018Review
- Methane utilization in Methylomicrobium alcaliphilum 20ZScientific reports · 2018Article
- Synthesis of arborane triterpenols by a bacterial oxidosqualene cyclase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Hopanoid-free Methylobacterium extorquens DM4 overproduces carotenoids and has widespread growth impairment.PloS one · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tetrahymanol is a polycyclic triterpenoid lipid first discovered in the ciliate Tetrahymena pyriformis whose potential diagenetic product, gammacerane, is often used as a biomarker for water column stratification in ancient ecosystems. Bacteria are also a potential source of tetrahymanol, but neither the distribution of this lipid in extant bacteria nor the significance of bacterial tetrahymanol synthesis for interpreting gammacerane biosignatures is known. Here we couple comparative genomics with genetic and lipid analyses to link a protein of unknown function to tetrahymanol synthesis in bacteria. This tetrahymanol synthase (Ths) is found in a variety of bacterial genomes, including aerobic methanotrophs, nitrite-oxidizers, and sulfate-reducers, and in a subset of aquatic and terrestrial metagenomes. Thus, the potential to produce tetrahymanol is more widespread in the bacterial domain than previously thought. However, Ths is not encoded in any eukaryotic genomes, nor is it homologous to eukaryotic squalene-tetrahymanol cyclase, which catalyzes the cyclization of squalene directly to tetrahymanol. Rather, heterologous expression studies suggest that bacteria couple the cyclization of squalene to a hopene molecule by squalene-hopene cyclase with a subsequent Ths-dependent ring expansion to form tetrahymanol. Thus, bacteria and eukaryotes have evolved distinct biochemical mechanisms for producing tetrahymanol.
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