At least three groups of anaerobic eukaryotes lack mitochondria and instead contain hydrogenosomes, peculiar organelles that make energy and excrete hydrogen. Published data indicate that ciliate and trichomonad hydrogenosomes share common ancestry with mitochondria, but the evolutionary origins of fungal hydrogenosomes have been controversial. We have now isolated full-length genes for heat shock proteins 60 and 70 from the anaerobic fungus Neocallimastix patriciarum, which phylogenetic analyses reveal share common ancestry with mitochondrial orthologues. In aerobic organisms these proteins function in mitochondrial import and protein folding. Homologous antibodies demonstrated the localization of both proteins to fungal hydrogenosomes. Moreover, both sequences contain amino-terminal extensions that in heterologous targeting experiments were shown to be necessary and sufficient to locate both proteins and green fluorescent protein to the mitochondria of mammalian cells. This finding, that fungal hydrogenosomes use mitochondrial targeting signals to import two proteins of mitochondrial ancestry that play key roles in aerobic mitochondria, provides further strong evidence that the fungal organelle is also of mitochondrial ancestry. The extraordinary capacity of eukaryotes to repeatedly evolve hydrogen-producing organelles apparently reflects a general ability to modify the biochemistry of the mitochondrial compartment.

Fungal hydrogenosomes contain mitochondrial heat-shock proteins / M. van der Giezen, G.M. Birdsey, D.S. Horner, J Lucocq, P.L. Dyall, M. Benchimol, C.J. Danpure, T.M. Embley. - In: MOLECULAR BIOLOGY AND EVOLUTION. - ISSN 0737-4038. - 20:7(2003), pp. 1051-1061. [10.1093/molbev/msg103]

Fungal hydrogenosomes contain mitochondrial heat-shock proteins

D.S. Horner;
2003

Abstract

At least three groups of anaerobic eukaryotes lack mitochondria and instead contain hydrogenosomes, peculiar organelles that make energy and excrete hydrogen. Published data indicate that ciliate and trichomonad hydrogenosomes share common ancestry with mitochondria, but the evolutionary origins of fungal hydrogenosomes have been controversial. We have now isolated full-length genes for heat shock proteins 60 and 70 from the anaerobic fungus Neocallimastix patriciarum, which phylogenetic analyses reveal share common ancestry with mitochondrial orthologues. In aerobic organisms these proteins function in mitochondrial import and protein folding. Homologous antibodies demonstrated the localization of both proteins to fungal hydrogenosomes. Moreover, both sequences contain amino-terminal extensions that in heterologous targeting experiments were shown to be necessary and sufficient to locate both proteins and green fluorescent protein to the mitochondria of mammalian cells. This finding, that fungal hydrogenosomes use mitochondrial targeting signals to import two proteins of mitochondrial ancestry that play key roles in aerobic mitochondria, provides further strong evidence that the fungal organelle is also of mitochondrial ancestry. The extraordinary capacity of eukaryotes to repeatedly evolve hydrogen-producing organelles apparently reflects a general ability to modify the biochemistry of the mitochondrial compartment.
English
heat-shock proteins ; hydrogenosomes ; mitochondria ; anaerobic eukaryotes ; evolution
Articolo
Sì, ma tipo non specificato
2003
Oxford University Press
20
7
1051
1061
Periodico con rilevanza internazionale
info:eu-repo/semantics/article
Fungal hydrogenosomes contain mitochondrial heat-shock proteins / M. van der Giezen, G.M. Birdsey, D.S. Horner, J Lucocq, P.L. Dyall, M. Benchimol, C.J. Danpure, T.M. Embley. - In: MOLECULAR BIOLOGY AND EVOLUTION. - ISSN 0737-4038. - 20:7(2003), pp. 1051-1061. [10.1093/molbev/msg103]
none
Prodotti della ricerca::01 - Articolo su periodico
8
262
Article (author)
si
M. van der Giezen, G.M. Birdsey, D.S. Horner, J Lucocq, P.L. Dyall, M. Benchimol, C.J. Danpure, T.M. Embley
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/25043
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