Details
| Original language | English |
|---|---|
| Pages (from-to) | 145-153 |
| Number of pages | 9 |
| Journal | Molecular biology and evolution |
| Volume | 20 |
| Issue number | 1 |
| Publication status | Published - 1 Jan 2003 |
Abstract
In eubacteria, the respiratory bc1 complex (complex III) consists of three or four different subunits, whereas that of mitochondria, which have descended from an α-proteobacterial endosymbiont, contains about seven additional subunits. To understand better how mitochondrial protein complexes evolved from their simpler bacterial predecessors, we purified complex III of Seculamonas ecuadoriensis, a member of the jakobid protists, which possess the most bacteria-like mitochondrial genomes known. The S. ecuadoriensis complex III has an apparent molecular mass of 460 kDa and exhibits antimycin-sensitive quinol:cytochrome c oxidoreductase activity. It is composed of at least eight subunits between 6 and 46 kDa in size, including two large "core" subunits and the three "respiratory" subunits. The molecular mass of the S. ecuadoriensis bC1 complex is slightly lower than that reported for other eukaryotes, but about 2× as large as complex III in bacteria. This indicates that the departure from the small bacteria-like complex III took place at an early stage in mitochondrial evolution, prior to the divergence of jakobids. We posit that the recruitment of additional subunits in mitochondrial respiratory complexes is a consequence of the migration of originally et α-proteobacterial genes to the nucleus.
Keywords
- Bc complex, Evolution, Jakobid flagellates, Mitochondria, Seculamonas ecuadoriensis
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Ecology, Evolution, Behavior and Systematics
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
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In: Molecular biology and evolution, Vol. 20, No. 1, 01.01.2003, p. 145-153.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Structure of the bc1 Complex from Seculamonas ecuadoriensis, a Jakobid Flagellate with an Ancestral Mitochondrial Genome
AU - Marx, Stefanie
AU - Baumgärtner, Maja
AU - Kunnan, Sivakumar
AU - Braun, Hans Peter
AU - Lang, B. Franz
AU - Burger, Gertraud
PY - 2003/1/1
Y1 - 2003/1/1
N2 - In eubacteria, the respiratory bc1 complex (complex III) consists of three or four different subunits, whereas that of mitochondria, which have descended from an α-proteobacterial endosymbiont, contains about seven additional subunits. To understand better how mitochondrial protein complexes evolved from their simpler bacterial predecessors, we purified complex III of Seculamonas ecuadoriensis, a member of the jakobid protists, which possess the most bacteria-like mitochondrial genomes known. The S. ecuadoriensis complex III has an apparent molecular mass of 460 kDa and exhibits antimycin-sensitive quinol:cytochrome c oxidoreductase activity. It is composed of at least eight subunits between 6 and 46 kDa in size, including two large "core" subunits and the three "respiratory" subunits. The molecular mass of the S. ecuadoriensis bC1 complex is slightly lower than that reported for other eukaryotes, but about 2× as large as complex III in bacteria. This indicates that the departure from the small bacteria-like complex III took place at an early stage in mitochondrial evolution, prior to the divergence of jakobids. We posit that the recruitment of additional subunits in mitochondrial respiratory complexes is a consequence of the migration of originally et α-proteobacterial genes to the nucleus.
AB - In eubacteria, the respiratory bc1 complex (complex III) consists of three or four different subunits, whereas that of mitochondria, which have descended from an α-proteobacterial endosymbiont, contains about seven additional subunits. To understand better how mitochondrial protein complexes evolved from their simpler bacterial predecessors, we purified complex III of Seculamonas ecuadoriensis, a member of the jakobid protists, which possess the most bacteria-like mitochondrial genomes known. The S. ecuadoriensis complex III has an apparent molecular mass of 460 kDa and exhibits antimycin-sensitive quinol:cytochrome c oxidoreductase activity. It is composed of at least eight subunits between 6 and 46 kDa in size, including two large "core" subunits and the three "respiratory" subunits. The molecular mass of the S. ecuadoriensis bC1 complex is slightly lower than that reported for other eukaryotes, but about 2× as large as complex III in bacteria. This indicates that the departure from the small bacteria-like complex III took place at an early stage in mitochondrial evolution, prior to the divergence of jakobids. We posit that the recruitment of additional subunits in mitochondrial respiratory complexes is a consequence of the migration of originally et α-proteobacterial genes to the nucleus.
KW - Bc complex
KW - Evolution
KW - Jakobid flagellates
KW - Mitochondria
KW - Seculamonas ecuadoriensis
UR - http://www.scopus.com/inward/record.url?scp=0037225494&partnerID=8YFLogxK
U2 - 10.1093/molbev/msg016
DO - 10.1093/molbev/msg016
M3 - Article
AN - SCOPUS:0037225494
VL - 20
SP - 145
EP - 153
JO - Molecular biology and evolution
JF - Molecular biology and evolution
SN - 0737-4038
IS - 1
ER -