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Decoding the chemical language of fungi: genome mining and untargeted metabolomics uncover terpene chemical diversity.
mSystems
April 2024
Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.
Ectomycorrhizal fungi establish mutually beneficial relationships with trees, trading nutrients for carbon. are ectomycorrhizal fungi that are critical to the health of boreal and temperate forest ecosystems. Comparative genomics has identified a high number of non-ribosomal peptide synthetase and terpene biosynthetic gene clusters (BGC) potentially involved in fungal competition and communication.
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- Ectomycorrhizal fungi form beneficial relationships with trees, exchanging nutrients for carbon and playing a key role in forest ecosystems.
- Comparative genomics revealed many non-ribosomal peptide synthetase and terpene biosynthetic gene clusters (BGCs) in these fungi, but their functions remained unclear until this study.
- Using co-culture and metabolomics techniques, researchers identified diverse metabolites produced by three fungal species, highlighting the significance of terpenes in fungal communication and forest health.
ER membrane-localized oxidoreductase Ero1 is required for disulfide bond formation in the rice endosperm.
Proc Natl Acad Sci U S A
August 2009
Division of Plant Sciences, National Institute of Agrobiological Sciences, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602, Japan.
The developing endosperm of rice (Oryza sativa, Os) synthesizes a large amount of storage proteins on the rough (r)ER. The major storage proteins, glutelins and prolamins, contain either intra or intermolecular disulfide bonds, and oxidative protein folding is necessary for the sorting of the proteins to the protein bodies. Here, we investigated an electron transfer pathway for the formation of protein disulfide bonds in the rER of the rice endosperm, focusing on the roles of the thiol-disulfide oxidoreductase, OsEro1.
View Article and Find Full Text PDFBinding of polymyxin B nonapeptide to gram-negative bacteria.
Antimicrob Agents Chemother
April 1985
The binding of the outer membrane-disorganizing peptide polymyxin B nonapeptide (PMBN) to gram-negative bacteria was studied by using tritium-labeled PMBN. Smooth Salmonella typhimurium had a binding capacity of ca. 6 nmol of PMBN per mg (dry weight) of bacteria, which corresponds to ca.
View Article and Find Full Text PDFEM49 is a family of similar peptide antibiotics, each an octapeptide acylated with a beta-hydroxy fatty acid. This paper described the determination of the structure of the fatty acyl residue, the selective removal of this residue from the peptide portion of the molecule, and the sequential analysis of the peptide by the EDMAN method. The structure of EM49, 1, is derived by this degradation.
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