This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Remodeling may bring to mind construction crews and scaffolding, but the process is far from unique to buildings. Even molecules can be remodeled.
Pandorachelins, newly discovered molecules produced by Pandoraea bacteria, are one example. These findings from researchers at the Leibniz Institute for Natural Product Research and Infection Biology Hans Knöll Institute (Leibniz-HKI) and the Cluster of Excellence "Balance of the Microverse" at the University of Jena were published in Angewandte Chemie International Edition. Pandorachelins are siderophores: molecules that help bacteria capture, or chelate, the iron they need to survive.
But while siderophores may be best known for their iron-binding abilities, Leibniz-HKI researchers in Jena have discovered that acquiring iron isn't all pandorachelins can do. Enzymatic remodeling allows pandorachelins to take on a new role. This transformation may make bacteria better suited to their environments.
"We discovered that certain bacteria can transform a peptide with minor changes into another peptide, changing its function from supporting movement to capturing iron more efficiently. This remarkable transformation shows how bacteria can adapt their molecular tools to meet different needs," says Elena Herzog, who co-authored the paper as part of her doctoral work alongside postdoctoral researcher Keishi Ishida in the lab of Christian Hertweck, department head at Leibniz-HKI and professor at Friedrich Schiller University Jena. Early bioinformatic analysis led researchers to predict that Pandoraea bacteria produce a peptide with a fatty acid.
However, upon discovering pandorachelin A, Ishida and Herzog were surprised to find that the fatty acid was nowhere to be found. The search for this missing fatty acid led them to pandorachelin B, a lipocyclopeptide. The group's research revealed key differences in the structures of pandorachelin A and B.
They discovered that pandorachelin B becomes pandorachelin A after an acylase, PdnM, cuts off pandorachelin B's lipid tail, triggering an internal rearrangement that leads to a head-to-tail fusion. This rearrangement changes more than pandorachelin's form. It also alters its function.
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