ArticleProceedings of the National Academy of Sciences of the United States of America2024
Identification of two archaeal GDGT lipid-modifying proteins reveals diverse microbes capable of GMGT biosynthesis and modification.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Mechanistic insight into radicalNatural product reports · 2026Review
- Novel Extended Tetraether Lipids Found in a High-COEnvironmental microbiology · 2026Article
- Decoding the Chemical Language of Ribosomally Synthesized and Post-Translationally Modified Peptides from the Untapped Archaea Domain.Angewandte Chemie (International ed. in English) · 2025Article
- Cyclization of archaeal membrane lipids impacts membrane protein activity and archaellum formation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Discovering Hidden Archaeal and Bacterial Lipid Producers in a Euxinic Marine System.Environmental microbiology · 2025Article
- Identification of two archaeal GDGT lipid-modifying proteins reveals diverse microbes capable of GMGT biosynthesis and modification.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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Authors and funding
4 authors.
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Abstract
Archaea produce unique membrane-spanning lipids (MSLs), termed glycerol dialkyl glycerol tetraethers (GDGTs), which aid in adaptive responses to various environmental challenges. GDGTs can be modified through cyclization, cross-linking, methylation, hydroxylation, and desaturation, resulting in structurally distinct GDGT lipids. Here, we report the identification of radical SAM proteins responsible for two of these modifications-a glycerol monoalkyl glycerol tetraether (GMGT) synthase (Gms), responsible for covalently cross-linking the two hydrocarbon tails of a GDGT to produce GMGTs, and a GMGT methylase (Gmm), capable of methylating the core hydrocarbon tail. Heterologous expression of Gms proteins from various archaea in
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