Phosphorylation of Phosphoenolpyruvate carboxylase is not essential fo high photosynthetic rates in the C4 species laveria bidentis 1[OA]
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Furumoto, Tsuyoshi; Izui, Katsura; Quinn, Vanda; Furbank, Robert Thomas; von Caemmerer, Susanne
Description
Phosphoenolpyruvate carboxylase (PEPC; EC4.1.1.31) plays a key role during C4 photosynthesis. The enzyme is activated by metabolites such as glucose-6-phosphate and inhibited by malate. This metabolite sensitivity is modulated by the reversible phosphorylation of a conserved serine residue near the N terminus in response to light. The phosphorylation of PEPC is modulated by a protein kinase specific to PEPC (PEPC-PK). To explore the role PEPC-PK plays in the regulation of C4 photosynthetic CO2...[Show more]
dc.contributor.author | Furumoto, Tsuyoshi | |
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dc.contributor.author | Izui, Katsura | |
dc.contributor.author | Quinn, Vanda | |
dc.contributor.author | Furbank, Robert Thomas | |
dc.contributor.author | von Caemmerer, Susanne | |
dc.date.accessioned | 2015-12-10T22:39:32Z | |
dc.identifier.issn | 0032-0889 | |
dc.identifier.uri | http://hdl.handle.net/1885/57222 | |
dc.description.abstract | Phosphoenolpyruvate carboxylase (PEPC; EC4.1.1.31) plays a key role during C4 photosynthesis. The enzyme is activated by metabolites such as glucose-6-phosphate and inhibited by malate. This metabolite sensitivity is modulated by the reversible phosphorylation of a conserved serine residue near the N terminus in response to light. The phosphorylation of PEPC is modulated by a protein kinase specific to PEPC (PEPC-PK). To explore the role PEPC-PK plays in the regulation of C4 photosynthetic CO2 fixation, we have transformed Flaveria bidentis (a C4 dicot) with antisense or RNA interference constructs targeted at the mRNA of this PEPC-PK. We generated several independent transgenic lines where PEPC is not phosphorylated in the light, demonstrating that this PEPC-PK is essential for the phosphorylation of PEPC in vivo. Malate sensitivity of PEPC extracted from these transgenic lines in the light was similar to the malate sensitivity of PEPC extracted from darkened wild-type leaves but greater than the malate sensitivity observed in PEPC extracted from wild-type leaves in the light, confirming the link between PEPC phosphorylation and the degree of malate inhibition. There were, however, no differences in the CO2 and light response of CO2 assimilation rates between wild-type plants and transgenic plants with low PEPC phosphorylation, showing that phosphorylation of PEPC in the light is not essential for efficient C4 photosynthesis for plants grown under standard glasshouse conditions. This raises the intriguing question of what role this complexly regulated reversible phosphorylation of PEPC plays in C 4 photosynthesis. | |
dc.publisher | American Society of Plant Biologists | |
dc.source | Plant Physiology | |
dc.subject | Keywords: Malate inhibition; Metabolite sensitivity; Protein kinase; Glucose; Metabolites; Phosphorylation; Photosynthesis; Enzyme activity; carbon dioxide; malic acid; malic acid derivative; messenger RNA; phosphoenolpyruvate carboxylase; phosphoenolpyruvate carbo | |
dc.title | Phosphorylation of Phosphoenolpyruvate carboxylase is not essential fo high photosynthetic rates in the C4 species laveria bidentis 1[OA] | |
dc.type | Journal article | |
local.description.notes | Imported from ARIES | |
local.identifier.citationvolume | 144 | |
dc.date.issued | 2007 | |
local.identifier.absfor | 060705 - Plant Physiology | |
local.identifier.absfor | 060107 - Enzymes | |
local.identifier.ariespublication | u9204316xPUB391 | |
local.type.status | Published Version | |
local.contributor.affiliation | Furumoto, Tsuyoshi, Hiroshima University | |
local.contributor.affiliation | Izui, Katsura, Kinki University | |
local.contributor.affiliation | Quinn, Vanda, College of Medicine, Biology and Environment, ANU | |
local.contributor.affiliation | Furbank, Robert Thomas, CSIRO Division of Plant Industry | |
local.contributor.affiliation | von Caemmerer, Susanne, College of Medicine, Biology and Environment, ANU | |
local.description.embargo | 2037-12-31 | |
local.bibliographicCitation.startpage | 1936 | |
local.bibliographicCitation.lastpage | 1945 | |
local.identifier.doi | 10.1104/pp.107.102541 | |
dc.date.updated | 2015-12-09T10:52:18Z | |
local.identifier.scopusID | 2-s2.0-34547880040 | |
Collections | ANU Research Publications |
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