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Prokaryotic origins for the mitochondrial alternative oxidase and plastid terminal oxidase nuclear genes
- Source :
- FEBS letters. 555(3)
- Publication Year :
- 2003
-
Abstract
- The mitochondrial alternative oxidase is a diiron carboxylate quinol oxidase (Dox) found in plants and some fungi and protists, but not animals. The plastid terminal oxidase is distantly related to alternative oxidase and is most likely also a Dox protein. Database searches revealed that the α-proteobacterium Novosphingobium aromaticivorans and the cyanobacteria Nostoc sp. PCC7120, Synechococcus sp. WH8102 and Prochlorococcus marinus subsp. pastoris CCMP1378 each possess a Dox homolog. Each prokaryotic protein conforms to the current structural models of the Dox active site and phylogenetic analyses suggest that the eukaryotic Dox genes arose from an ancestral prokaryotic gene.
- Subjects :
- 0106 biological sciences
Cyanobacteria
Alternative oxidase
Nostoc
Nuclear gene
Novosphingobium
Molecular Sequence Data
Biophysics
Molecular phylogeny
macromolecular substances
01 natural sciences
Biochemistry
Plastid terminal oxidase
Mitochondrial Proteins
03 medical and health sciences
Structural Biology
Proteobacteria
polycyclic compounds
Genetics
Amino Acid Sequence
Plastids
Molecular Biology
Gene
Phylogeny
030304 developmental biology
Alphaproteobacteria
Plant Proteins
0303 health sciences
Binding Sites
biology
Phylogenetic tree
Sequence Homology, Amino Acid
fungi
IMMUTANS
technology, industry, and agriculture
Diiron carboxylate proteins
Cell Biology
biology.organism_classification
Mitochondria
carbohydrates (lipids)
Prokaryotic Cells
Oxidoreductases
Sequence Alignment
010606 plant biology & botany
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 555
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....8ab95bc1c8a00f9259ca43292a091acc