Natalie Niessen, Jörg Soppa
Journal: Biomolecules 2021;10(7):1072
PMID: 32709147
Iron is part of many redox and other enzymes and, thus, it is essential for all living beings. Many oxic environments have extremely low concentrations of free iron. Therefore, many prokaryotic species evolved siderophores, i.e., small organic molecules that complex Fe with very high affinity. Siderophores of bacteria are intensely studied, in contrast to those of archaea. The haloarchaeon contains a gene cluster that putatively encodes siderophore biosynthesis genes, including four iron uptake chelate () genes. Underscoring this hypothesis, Northern blot analyses revealed that a hexacistronic transcript is generated that is highly induced under iron starvation. A quadruple deletion mutant was generated, which had a growth defect solely at very low concentrations of Fe, not Fe. Two experimental approaches showed that the wild type produced and exported an Fe-specific siderophore under low iron concentrations, in contrast to the deletion mutant. Bioinformatic analyses revealed that haloarchaea obtained the gene cluster by lateral transfer from bacteria and enabled the prediction of enzymatic functions of all six gene products. Notably, a biosynthetic pathway is proposed that starts with aspartic acid, uses several group donors and citrate, and leads to the hydroxamate siderophore Schizokinen.
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