Mixing and matching siderophore clusters: Structure and biosynthesis of serratiochelins from serratia sp. V4

Mohammad R. Seyedsayamdost, Sara Cleto, Gavin Carr, Hera Vlamakis, Maria João Vieira, Roberto Kolter, Jon Clardy

Research output: Contribution to journalArticlepeer-review

45 Scopus citations


Interrogation of the evolutionary history underlying the remarkable structures and biological activities of natural products has been complicated by not knowing the functions they have evolved to fulfill. Siderophores-soluble, low molecular weight compounds-have an easily understood and measured function: acquiring iron from the environment. Bacteria engage in a fierce competition to acquire iron, which rewards the production of siderophores that bind iron tightly and cannot be used or pirated by competitors. The structures and biosyntheses of "odd" siderophores can reveal the evolutionary strategy that led to their creation. We report a new Serratia strain that produces serratiochelin and an analog of serratiochelin. A genetic approach located the serratiochelin gene cluster, and targeted mutations in several genes implicated in serratiochelin biosynthesis were generated. Bioinformatic analyses and mutagenesis results demonstrate that genes from two well-known siderophore clusters, the Escherichia coli enterobactin cluster and the Vibrio cholera vibriobactin cluster, were shuffled to produce a new siderophore biosynthetic pathway. These results highlight how modular siderophore gene clusters can be mixed and matched during evolution to generate structural diversity in siderophores.

Original languageEnglish (US)
Pages (from-to)13550-13553
Number of pages4
JournalJournal of the American Chemical Society
Issue number33
StatePublished - Aug 22 2012

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • Biochemistry
  • Catalysis
  • Colloid and Surface Chemistry


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