UNIGE document Scientific Article
previous document  unige:13154  next document
add to browser collection
Title

Prokaryotic origins of the non-animal peroxidase superfamily and organelle-mediated transmission to eukaryotes

Authors
Bakalovic, Nenad
Teixeira, Felipe Karam
Margis-Pinheiro, Marcia
Published in Genomics. 2007, vol. 89, no. 5, p. 567-79
Abstract Members of the superfamily of plant, fungal, and bacterial peroxidases are known to be present in a wide variety of living organisms. Extensive searching within sequencing projects identified organisms containing sequences of this superfamily. Class I peroxidases, cytochrome c peroxidase (CcP), ascorbate peroxidase (APx), and catalase peroxidase (CP), are known to be present in bacteria, fungi, and plants, but have now been found in various protists. CcP sequences were detected in most mitochondria-possessing organisms except for green plants, which possess only ascorbate peroxidases. APx sequences had previously been observed only in green plants but were also found in chloroplastic protists, which acquired chloroplasts by secondary endosymbiosis. CP sequences that are known to be present in prokaryotes and in Ascomycetes were also detected in some Basidiomycetes and occasionally in some protists. Class II peroxidases are involved in lignin biodegradation and are found only in the Homobasidiomycetes. In fact class II peroxidases were identified in only three orders, although degenerate forms were found in different Pezizomycota orders. Class III peroxidases are specific for higher plants, and their evolution is thought to be related to the emergence of the land plants. We have found, however, that class III peroxidases are present in some green algae, which predate land colonization. The presence of peroxidases in all major phyla (except vertebrates) makes them powerful marker genes for understanding the early evolutionary events that led to the appearance of the ancestors of each eukaryotic group.
Keywords AnimalsBacteria/enzymologyCytochrome-c Peroxidase/classification/geneticsEukaryotic Cells/enzymologyEvolution, MolecularFungi/enzymologyPeroxidases/classification/geneticsPhylogenyPlants/enzymology
Stable URL https://archive-ouverte.unige.ch/unige:13154
Full text
Article (Published version) (543 Kb) - document accessible for UNIGE members only Limited access to UNIGE
Identifiers
PMID: 17355904
Structures

202 hits

4 downloads

Update

Deposited on : 2011-01-11

Export document
Format :
Citation style :