Divergent mitochondrial respiratory chains in phototrophic relatives of apicomplexan parasites

Handle URI:
http://hdl.handle.net/10754/564048
Title:
Divergent mitochondrial respiratory chains in phototrophic relatives of apicomplexan parasites
Authors:
Flegontov, Pavel; Michálek, Jan; Janouškovec, Jan; Lai, De Hua; Jirků, Milan; Hajdušková, Eva; Tomčala, Aleš; Otto, Thomas D.; Keeling, Patrick J.; Pain, Arnab ( 0000-0002-1755-2819 ) ; Oborník, Miroslav; Lukeš, J.
Abstract:
Four respiratory complexes and ATP-synthase represent central functional units in mitochondria. In some mitochondria and derived anaerobic organelles, a few or all of these respiratory complexes have been lost during evolution. We show that the respiratory chain of Chromera velia, a phototrophic relative of parasitic apicomplexans, lacks complexes I and III, making it a uniquely reduced aerobic mitochondrion. In Chromera, putative lactate:cytochrome c oxidoreductases are predicted to transfer electrons from lactate to cytochrome c, rendering complex III unnecessary. The mitochondrial genome of Chromera has the smallest known protein-coding capacity of all mitochondria, encoding just cox1 and cox3 on heterogeneous linear molecules. In contrast, another photosynthetic relative of apicomplexans, Vitrella brassicaformis, retains the same set of genes as apicomplexans and dinoflagellates (cox1, cox3, and cob). © The Author 2015. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Computational Bioscience Research Center (CBRC); Pathogen Genomics Laboratory
Publisher:
Oxford University Press (OUP)
Journal:
Molecular Biology and Evolution
Issue Date:
6-Feb-2015
DOI:
10.1093/molbev/msv021
Type:
Article
ISSN:
07374038
Sponsors:
The authors thank the KAUST Bioscience Core Laboratory personnel for sequencing Illumina libraries used in this project, Evgeny S. Gerasimov (Institute for Information Transmission Problems, Russian Academy of Sciences, Moscow) and Martin Kolisko (University of British Columbia, Vancouver) for help with sequence analysis, Oldrich Benada (Institute of Microbiology, Prague) for help with electron microscopy, Anton Horvath (Comenius University, Bratislava), Dave Speijer (University of Amsterdam, Amsterdam), and Ivan Hrdy (Charles University, Prague) for useful comments. This work was supported by Czech Science Foundation grants P506/12/1522, 13-33039S (support for J.M.) and P501/12/G055 (support for A.T.) to M.O., project Algatech (CZ.1.05/2.1.00/03.0110) to M.O., FP7 agreement 316304 to M.O. and J.L., the KAUST award FIC/2010/09 to A.P., M.O. and J.L., and by a grant from the Canadian Institutes for Health Research to P.J.K. and J.L. is also supported by the Praemium Academiae, and P.F. by a grant of the Moravian-Silesian region (project MSK2013-DT1) and by Russian Foundation for Basic Research (project 14-04-31936). P.J.K. and J.L. are Senior Fellows and J.J. is a Global Scholar at the Canadian Institute for Advanced Research, and P.J.K. was supported by a Fellowship from the John Simon Guggenheim Foundation.
Appears in Collections:
Articles; Bioscience Program; Computational Bioscience Research Center (CBRC); Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorFlegontov, Pavelen
dc.contributor.authorMichálek, Janen
dc.contributor.authorJanouškovec, Janen
dc.contributor.authorLai, De Huaen
dc.contributor.authorJirků, Milanen
dc.contributor.authorHajdušková, Evaen
dc.contributor.authorTomčala, Alešen
dc.contributor.authorOtto, Thomas D.en
dc.contributor.authorKeeling, Patrick J.en
dc.contributor.authorPain, Arnaben
dc.contributor.authorOborník, Miroslaven
dc.contributor.authorLukeš, J.en
dc.date.accessioned2015-08-03T12:29:47Zen
dc.date.available2015-08-03T12:29:47Zen
dc.date.issued2015-02-06en
dc.identifier.issn07374038en
dc.identifier.doi10.1093/molbev/msv021en
dc.identifier.urihttp://hdl.handle.net/10754/564048en
dc.description.abstractFour respiratory complexes and ATP-synthase represent central functional units in mitochondria. In some mitochondria and derived anaerobic organelles, a few or all of these respiratory complexes have been lost during evolution. We show that the respiratory chain of Chromera velia, a phototrophic relative of parasitic apicomplexans, lacks complexes I and III, making it a uniquely reduced aerobic mitochondrion. In Chromera, putative lactate:cytochrome c oxidoreductases are predicted to transfer electrons from lactate to cytochrome c, rendering complex III unnecessary. The mitochondrial genome of Chromera has the smallest known protein-coding capacity of all mitochondria, encoding just cox1 and cox3 on heterogeneous linear molecules. In contrast, another photosynthetic relative of apicomplexans, Vitrella brassicaformis, retains the same set of genes as apicomplexans and dinoflagellates (cox1, cox3, and cob). © The Author 2015. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution.en
dc.description.sponsorshipThe authors thank the KAUST Bioscience Core Laboratory personnel for sequencing Illumina libraries used in this project, Evgeny S. Gerasimov (Institute for Information Transmission Problems, Russian Academy of Sciences, Moscow) and Martin Kolisko (University of British Columbia, Vancouver) for help with sequence analysis, Oldrich Benada (Institute of Microbiology, Prague) for help with electron microscopy, Anton Horvath (Comenius University, Bratislava), Dave Speijer (University of Amsterdam, Amsterdam), and Ivan Hrdy (Charles University, Prague) for useful comments. This work was supported by Czech Science Foundation grants P506/12/1522, 13-33039S (support for J.M.) and P501/12/G055 (support for A.T.) to M.O., project Algatech (CZ.1.05/2.1.00/03.0110) to M.O., FP7 agreement 316304 to M.O. and J.L., the KAUST award FIC/2010/09 to A.P., M.O. and J.L., and by a grant from the Canadian Institutes for Health Research to P.J.K. and J.L. is also supported by the Praemium Academiae, and P.F. by a grant of the Moravian-Silesian region (project MSK2013-DT1) and by Russian Foundation for Basic Research (project 14-04-31936). P.J.K. and J.L. are Senior Fellows and J.J. is a Global Scholar at the Canadian Institute for Advanced Research, and P.J.K. was supported by a Fellowship from the John Simon Guggenheim Foundation.en
dc.publisherOxford University Press (OUP)en
dc.subjectanaerobic metabolismen
dc.subjectApicomplexaen
dc.subjectChromeraen
dc.subjectevolutionen
dc.subjectrespiratory chainen
dc.subjectVitrellaen
dc.titleDivergent mitochondrial respiratory chains in phototrophic relatives of apicomplexan parasitesen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentBioscience Programen
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.contributor.departmentPathogen Genomics Laboratoryen
dc.identifier.journalMolecular Biology and Evolutionen
dc.contributor.institutionInstitute of Parasitology, Biology Centre, Czech Academy of Sciences, České Budějovice, Czech Republicen
dc.contributor.institutionLife Science Research Centre, Department of Biology and Ecology, University of Ostrava, Ostrava, Czech Republicen
dc.contributor.institutionFaculty of Science, University of South Bohemia, České Budějovice, Czech Republicen
dc.contributor.institutionDepartment of Botany, University of BC, Vancouver, Canadaen
dc.contributor.institutionCanadian Institute for Advanced Research, Toronto, ON, Canadaen
dc.contributor.institutionWellcome Trust Sanger Institute, Hinxton, United Kingdomen
dc.contributor.institutionInstitute of Microbiology, Czech Academy of Sciences, Třeboň, Czech Republicen
kaust.authorPain, Arnaben
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