1887

Abstract

Fatty acid synthases (primary metabolism), non-ribosomal peptide synthases and polyketide synthases (secondary metabolism) contain phosphopantetheinyl (Ppant)-dependent carrier proteins that must be made functionally active by transfer of the 4′-Ppant moiety from coenzyme A. These reactions are usually catalysed by dedicated Ppant transferases. Although rich in Ppant-dependent carrier proteins, it was previously shown that possesses only one Ppant transferase, encoded by , which functions in both primary and secondary metabolism. Consistent with this notion are our findings that can genetically complement mutations in the and genes, encoding the apo-acyl carrier protein (ACP) synthase of fatty acid synthesis and a Ppant transferase of enterobactin synthesis, respectively. It also complements a mutation affecting a gene encoding a Ppant transferase essential for surfactin synthesis. A insertion mutant could only be constructed in a strain carrying the gene on a chromosomally integrated element , implying that the essentiality of is due to its requirement for activation of apo-ACP of fatty acid synthesis. The conditional mutant is non-fluorescent, does not produce pyoverdine and pyochelin, and does not grow in the presence of iron chelators. The data presented here for the first time confirm that PcpS plays an essential role in both fatty acid and siderophore metabolism.

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2004-04-01
2024-04-16
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