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Differential expression of recently duplicated PTOX genes in Glycine max during plant development and stress conditions
Plastid terminal oxidase (PTOX) is a chloroplast enzyme that catalyzes oxidation of plastoquinol (PQH 2 ) and reduction of molecular oxygen to water. Its function has been associated with carotenoid biosynthesis, chlororespiration and environmental stress responses in plants. In the majority of plan...
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Published in: | Journal of bioenergetics and biomembranes 2019-10, Vol.51 (5), p.355-370 |
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Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Plastid terminal oxidase (PTOX) is a chloroplast enzyme that catalyzes oxidation of plastoquinol (PQH
2
) and reduction of molecular oxygen to water. Its function has been associated with carotenoid biosynthesis, chlororespiration and environmental stress responses in plants. In the majority of plant species, a single gene encodes the protein and little is known about events of
PTOX
gene duplication and their implication to plant metabolism. Previously, two putative
PTOX
(
PTOX1
and
2
) genes were identified in
Glycine max
, but the evolutionary origin and the specific function of each gene was not explored. Phylogenetic analyses revealed that this gene duplication occurred apparently during speciation involving the
Glycine
genus ancestor, an event absent in all other available plant leguminous genomes. Gene expression evaluated by RT-qPCR and RNA-seq data revealed that both
PTOX
genes are ubiquitously expressed in
G. max
tissues, but their mRNA levels varied during development and stress conditions. In development,
PTOX1
was predominant in young tissues, while
PTOX2
was more expressed in aged tissues. Under stress conditions, the
PTOX
transcripts varied according to stress severity, i.e.,
PTOX1
mRNA was prevalent under mild or moderate stresses while
PTOX2
was predominant in drastic stresses. Despite the high identity between proteins (97%), molecular docking revealed that PTOX1 has higher affinity to substrate plastoquinol than PTOX2. Overall, our results indicate a functional relevance of this gene duplication in
G. max
metabolism, whereas
PTOX1
could be associated with chloroplast effectiveness and
PTOX2
to senescence and/or apoptosis. |
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ISSN: | 0145-479X 1573-6881 |
DOI: | 10.1007/s10863-019-09810-x |