Biogenesis of iron-sulphur clusters in amitochondriate and apicomplexan protists.
During the last 4 years there has been an enormous interest in the question how iron-sulphur ([Fe-S]) clusters, which are essential building blocks for life, are synthesised and assembled into apo-proteins, both in prokaryotes and in eukaryotes. The emerging picture is that the basic mechanism of this pathway has been well conserved during evolution. In yeast and probably all other eukaryotes the mitochondrion is the place where [Fe-S] clusters are synthesised, even for extramitochondrial [Fe-S] cluster-containing proteins, and a number of proteins have been functionally characterised to a certain extent within this pathway. However, almost nothing is known about this aspect in parasitic protists, although recent studies of amitochondriate protists and on the plastid-like organelle of apicomplexan parasites, the apicoplast, have started to change this. In this article I will summarise the current view of [Fe-S] cluster biogenesis in eukaryotes and discuss its implications for amitochondriate protists and for the plastid-like organelle of apicomplexan parasites.
FB Biology/Parasitology, Philipps-Universität Marburg, Karl-von-Frisch-Strasse, D-35032, Marburg, Germany. seeber@mailer.uni-marburg.de
Frank
F
Seeber
D000818:Animals; D016782:Apicomplexa / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D018407:Bacterial Physiological Phenomena; D056890:Eukaryota / Q000166:cytology / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000502:physiology; D007506:Iron-Sulfur Proteins / Q000096:biosynthesis* / Q000145:classification; D008928:Mitochondria / Q000378:metabolism; D008954:Models, Biological; D015003:Yeasts / Q000502:physiology
D007506:Iron-Sulfur Proteins