Ferricrocin functions as the main intracellular iron-storage compound in mycelia of Neurospora crassa

Biol Met. 1988;1(1):18-25. doi: 10.1007/BF01128013.

Abstract

Neurospora crassa produces several structurally distinct siderophores: coprogen, ferricrocin, ferrichrome C and some minor unknown compounds. Under conditions of iron starvation, desferricoprogen is the major extracellular siderophore whereas desferriferricrocin and desferriferichrome C are predominantly found intracellularly. Mössbauer spectroscopic analyses revealed that coprogen-bound iron is rapidly released after uptake in mycelia of the wild-type N. crassa 74A. The major intracellular target of iron distribution is desferriferricrocin. No ferritin-like iron pools could be detected. Ferricrocin functions as the main intracellular iron-storage peptide in mycelia of N. crassa. After uptake of ferricrocin in both the wild-type N. crassa 74A and the siderophore-free mutant N. crassa arg-5 ota aga, surprisingly little metabolization (11%) could be observed. Since ferricrocin is the main iron-storage compound in spores of N. crassa, we suggest that ferricrocin is stored in mycelia for inclusion into conidiospores.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Transport, Active
  • Ferrichrome / analogs & derivatives*
  • Ferrichrome / metabolism
  • Hydroxamic Acids / metabolism
  • Iron / metabolism
  • Iron Chelating Agents / metabolism
  • Mutation
  • Neurospora crassa / genetics
  • Neurospora crassa / metabolism*
  • Siderophores
  • Spectroscopy, Mossbauer
  • Spores, Fungal / metabolism

Substances

  • Hydroxamic Acids
  • Iron Chelating Agents
  • Siderophores
  • Ferrichrome
  • ferricrocin
  • coprogen
  • Iron