Comparison of the chloroplast peroxidase system in the chlorophyte Chlamydomonas reinhardtii, the bryophyte Physcomitrella patens, the lycophyte Selaginella moellendorffii and the seed plant Arabidopsis thaliana.
BACKGROUND
Oxygenic photosynthesis is accompanied by the formation of reactive oxygen species (ROS), which damage proteins, lipids, DNA and finally limit plant yield. The enzymes of the chloroplast antioxidant system are exclusively nuclear encoded. During evolution, plastid and mitochondrial genes were post-endosymbiotically transferred to the nucleus, adapted for eukaryotic gene expression and post-translational protein targeting and supplemented with genes of eukaryotic origin.


RESULTS
Here, the genomes of the green alga Chlamydomonas reinhardtii, the moss Physcomitrella patens, the lycophyte Selaginella moellendorffii and the seed plant Arabidopsis thaliana were screened for ORFs encoding chloroplast peroxidases. The identified genes were compared for their amino acid sequence similarities and gene structures. Stromal and thylakoid-bound ascorbate peroxidases (APx) share common splice sites demonstrating that they evolved from a common ancestral gene. In contrast to most cormophytes, our results predict that chloroplast APx activity is restricted to the stroma in Chlamydomonas and to thylakoids in Physcomitrella. The moss gene is of retrotransposonal origin.The exon-intron-structures of 2CP genes differ between chlorophytes and streptophytes indicating an independent evolution. According to amino acid sequence characteristics only the A-isoform of Chlamydomonas 2CP may be functionally equivalent to streptophyte 2CP, while the weakly expressed B- and C-isoforms show chlorophyte specific surfaces and amino acid sequence characteristics. The amino acid sequences of chloroplast PrxII are widely conserved between the investigated species. In the analyzed streptophytes, the genes are unspliced, but accumulated four introns in Chlamydomonas. A conserved splice site indicates also a common origin of chlorobiont PrxQ.The similarity of splice sites also demonstrates that streptophyte glutathione peroxidases (GPx) are of common origin. Besides a less related cysteine-type GPx, Chlamydomonas encodes two selenocysteine-type GPx. The latter were lost prior or during streptophyte evolution.


CONCLUSIONS
Throughout plant evolution, there was a strong selective pressure on maintaining the activity of all three investigated types of peroxidases in chloroplasts. APx evolved from a gene, which dates back to times before differentiation of chlorobionts into chlorophytes and streptophytes, while Prx and presumably also GPx gene patterns may have evolved independently in the streptophyte and chlorophyte branches.
Pitsch
Nicola T
NT
Plant Science Institute, Heinrich-Heine-University, Universitätsstrasse 1, 40225 Düsseldorf, Germany.
Witsch
Benjamin
B
Baier
Margarete
M
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D060387:Ascorbate Peroxidases; D019068:Bryopsida / Q000201:enzymology / Q000235:genetics; D016825:Chlamydomonas reinhardtii / Q000201:enzymology / Q000235:genetics; D002736:Chloroplasts / Q000201:enzymology*; D057225:Data Mining; D030562:Databases, Protein; D005091:Exons / Q000235:genetics; D018628:Gene Dosage; D018506:Gene Expression Regulation, Plant; D005979:Glutathione Peroxidase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007438:Introns / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D054464:Peroxiredoxins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D012639:Seeds / Q000235:genetics / Q000378:metabolism; D032503:Selaginellaceae / Q000201:enzymology / Q000235:genetics; D016415:Sequence Alignment
D010544:Peroxidases; D060387:Ascorbate Peroxidases; D054464:Peroxiredoxins; D005979:Glutathione Peroxidase