Minimal cytosolic iron-sulfur cluster assembly machinery ofGiardia intestinalisis partially associated with mitosomes

Autor: Pavel Doležal, Julius Lukeš, Jan Pyrih, Eva Pyrihová, Jan Tachezy, Karel Harant, Martin Kolisko, Darja Stojanovová, Andrew J. Roger, Somsuvro Basu, Alexander C. Haindrich
Rok vydání: 2016
Předmět:
Zdroj: Molecular Microbiology. 102:701-714
ISSN: 0950-382X
DOI: 10.1111/mmi.13487
Popis: Iron-sulfur (Fe-S) clusters are essential cofactors that enable proteins to transport electrons, sense signals, or catalyze chemical reactions. The maturation of dozens of Fe-S proteins in various compartments of every eukaryotic cell is driven by several assembly pathways. The ubiquitous cytosolic Fe-S cluster assembly (CIA) pathway, typically composed of eight highly conserved proteins, depends on mitochondrial Fe-S cluster assembly (ISC) machinery. Giardia intestinalis contains one of the smallest eukaryotic genomes and the mitosome, an extremely reduced mitochondrion. Because the only pathway known to be retained within this organelle is the synthesis of Fe-S clusters mediated by ISC machinery, a likely function of the mitosome is to cooperate with the CIA pathway. We investigated the cellular localization of CIA components in G. intestinalis and the origin and distribution of CIA-related components and Tah18-like proteins in other Metamonada. We show that orthologs of Tah18 and Dre2 are missing in these eukaryotes. In Giardia, all CIA components are exclusively cytosolic, with the important exception of Cia2 and two Nbp35 paralogs, which are present in the mitosomes. We propose that the dual localization of Cia2 and Nbp35 proteins in Giardia might represent a novel connection between the ISC and the CIA pathways.
Databáze: OpenAIRE
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