Effects of ectopically expressed hyperthermophilic archaeon (Pyrococcus furiosus) ribulose-1,5-bisphosphate carboxylase/oxygenase on tobacco photosynthesis

Pyrococcus furiosus is a hyperthermophilic archaeon. Its ribulose-1,5-bisphosphate carboxylase/oxygenase (PfRubisco) has only large subunit (L). PfRubisco has a novel (L₂)₅, decameric structure and it possesses higher carboxylase activity and thermotolerance. To assess the potential functionality of...

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Bibliographic Details
Published in:Photosynthetica 2013-09, Vol.51 (3), p.387-394
Main Authors: Li, X. -G, Yang, J, Wang, R, Tang, X. -F, Meng, J. -J, Qin, H. -J, Liu, X, Guo, F, Wan, S. -B
Format: Article
Language:English
Subjects:
Biomedical and Life Sciences
chlorophyll
chloroplasts
heat tolerance
leaves
Life Sciences
Nicotiana benthamiana
peas
photoinhibition
photosystem I
Plant Physiology
Pyrococcus furiosus
tobacco
ultrastructure
viruses
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Summary:Pyrococcus furiosus is a hyperthermophilic archaeon. Its ribulose-1,5-bisphosphate carboxylase/oxygenase (PfRubisco) has only large subunit (L). PfRubisco has a novel (L₂)₅, decameric structure and it possesses higher carboxylase activity and thermotolerance. To assess the potential functionality of PfRubisco in higher plants under high-temperature stress, PfRubisco coding sequence was transiently expressed in Nicotiana benthamiana by Pea early browning virus mediated ectopic expression. The transgenic PfRubisco plants produced chlorotic yellow stripes in their leaves. Relative to the control leaves, those with yellow stripes exhibited decreased net photosynthetic rate and chlorophyll content, altered chloroplast ultrastructure, and more severe photoinhibition of both photosystem I and II. We concluded that the ectopic expression of PfRubisco might disrupt the chloroplast development and function in N. benthamiana. The potential cause of the disruption was discussed.
ISSN:0300-3604
1573-9058
DOI:10.1007/s11099-013-0035-0