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Minimal cytosolic iron-sulfur cluster assembly machinery of Giardia intestinalis is partially associated with mitosomes
J. Pyrih, E. Pyrihová, M. Kolísko, D. Stojanovová, S. Basu, K. Harant, AC. Haindrich, P. Doležal, J. Lukeš, A. Roger, J. Tachezy,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články
NLK
Free Medical Journals
od 1997 do Před 18 měsíci
Wiley Free Content
od 1997 do Před 18 měsíci
PubMed
27582265
DOI
10.1111/mmi.13487
Knihovny.cz E-zdroje
- MeSH
- cytoplazma MeSH
- cytosol metabolismus MeSH
- Giardia lamblia genetika metabolismus MeSH
- mitochondriální proteiny metabolismus MeSH
- mitochondrie metabolismus MeSH
- proteiny obsahující železo a síru metabolismus MeSH
- síra metabolismus MeSH
- železo metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
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.
Department of Parasitology Charles University Prague Vestec 252 42 Czech Republic
Institute of Parasitology Biology Centre České Budějovice Budweis 37005 Czech Republic
Citace poskytuje Crossref.org
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- $a 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.
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- $a Pyrihová, Eva $u Department of Parasitology, Charles University in Prague, Vestec, 252 42, Czech Republic.
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- $a Haindrich, Alexander C $u Institute of Parasitology, Biology Centre, České Budějovice, Budweis, 37005, Czech Republic. Faculty of Sciences, University of South Bohemia, České Budějovice, Budweis, 37005, Czech Republic.
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- $a Lukeš, Julius $u Institute of Parasitology, Biology Centre, České Budějovice, Budweis, 37005, Czech Republic. Faculty of Sciences, University of South Bohemia, České Budějovice, Budweis, 37005, Czech Republic. Canadian Institute for Advanced Research, Toronto, ON, M5G 1Z8, Canada.
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- $a Roger, Andrew $u Centre for Comparative Genomics and Evolutionary Bioinformatics, Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, NS, B3H 4R2, Canada. Canadian Institute for Advanced Research, Toronto, ON, M5G 1Z8, Canada.
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