scholarly journals BHLH32 modulates several biochemical and morphological processes that respond to Pi starvation in Arabidopsis

2007 ◽  
Vol 405 (1) ◽  
pp. 191-198 ◽  
Author(s):  
Zhi-Hui Chen ◽  
Gillian A. Nimmo ◽  
Gareth I. Jenkins ◽  
Hugh G. Nimmo
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Sufficient Conditions ◽  
Negative Regulator ◽  
Phosphate Limitation ◽  
Pi Starvation ◽  
Transparent Testa ◽  
Root Hair Formation ◽  
Phosphoenolpyruvate Carboxylase Kinase ◽  
Morphological Processes ◽  
Arabidopsis Proteins

Pi (inorganic phosphate) limitation severely impairs plant growth and reduces crop yield. Hence plants have evolved several biochemical and morphological responses to Pi starvation that both enhance uptake and conserve use. The mechanisms involved in Pi sensing and signal transduction are not completely understood. In the present study we report that a previously uncharacterized transcription factor, BHLH32, acts as a negative regulator of a range of Pi starvation-induced processes in Arabidopsis. In bhlh32 mutant plants in Pi-sufficient conditions, expression of several Pi starvation-induced genes, formation of anthocyanins, total Pi content and root hair formation were all significantly increased compared with the wild-type. Among the genes negatively regulated by BHLH32 are those encoding PPCK (phosphoenolpyruvate carboxylase kinase), which is involved in modifying metabolism so that Pi is spared. The present study has shown that PPCK genes are rapidly induced by Pi starvation leading to increased phosphorylation of phosphoenolpyruvate carboxylase. Furthermore, several Arabidopsis proteins that regulate epidermal cell differentiation [TTG1 (TRANSPARENT TESTA GLABRA1), GL3 (GLABRA3) and EGL3 (ENHANCER OF GL3)] positively regulate PPCK gene expression in response to Pi starvation. BHLH32 can physically interact with TTG1 and GL3. We propose that BHLH32 interferes with the function of TTG1-containing complexes and thereby affects several biochemical and morphological processes that respond to Pi availability.

The unique phosphoenolpyruvate carboxylase kinase

2003 ◽  
Vol 41 (6-7) ◽  
pp. 541-547 ◽  
Author(s):  
Cristina Echevarria ◽  
Jean Vidal
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Phosphoenolpyruvate Carboxylase Kinase

Factors involved in the rise of phosphoenolpyruvate carboxylase-kinase activity caused by salinity in sorghum leaves

Planta ◽  
2013 ◽  
Vol 237 (5) ◽  
pp. 1401-1413 ◽  
Author(s):  
José A. Monreal ◽  
Cirenia Arias-Baldrich ◽  
Francisco Pérez-Montaño ◽  
Jacinto Gandullo ◽  
Cristina Echevarría ◽  
...  
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Kinase Activity ◽  
Phosphoenolpyruvate Carboxylase Kinase

How to tell the time: the regulation of phosphoenolpyruvate carboxylase in Crassulacean acid metabolism (CAM) plants

2003 ◽  
Vol 31 (3) ◽  
pp. 728-730 ◽  
Author(s):  
H.G. Nimmo
Keyword(s):  
Circadian Rhythms ◽  
Phosphoenolpyruvate Carboxylase ◽  
Crassulacean Acid Metabolism ◽  
Acid Metabolism ◽  
Circadian Oscillator ◽  
Cam Plants ◽  
Reversible Phosphorylation ◽  
Circadian Expression ◽  
Phosphoenolpyruvate Carboxylase Kinase ◽  
Co2 Metabolism

Crassulacean acid metabolism (CAM) plants exhibit persistent circadian rhythms of CO2 metabolism. These rhythms are driven by changes in the flux through phosphoenolpyruvate carboxylase, which is regulated by reversible phosphorylation in response to a circadian oscillator. This article reviews progress in our understanding of the circadian expression of phosphoenolpyruvate carboxylase kinase.

The inorganic carbon requirements for nitrogen assimilation

1991 ◽  
Vol 69 (5) ◽  
pp. 1139-1145 ◽  
Author(s):  
David H. Turpin ◽  
Greg C. Vanlerberghe ◽  
Alan M. Amory ◽  
Robert D. Guy
Keyword(s):  
Amino Acid ◽  
Phosphoenolpyruvate Carboxylase ◽  
Nitrogen Assimilation ◽  
Inorganic Carbon ◽  
Dissolved Inorganic Carbon ◽  
Sufficient Conditions ◽  
Acid Synthesis ◽  
Amino Acid Synthesis ◽  
Bisphosphate Carboxylase ◽  
N Assimilation

In the green alga Selenastrum minutum (Naeg.) Collins the assimilation of NH4+ into the full suite of protein amino acids requires at least three separate and distinct inorganic carbon fixing reactions, catalyzed by the enzymes ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco), phosphoenolpyruvate carboxylase (PEPC), and carbamoyl phosphate synthetase. In this paper we examine the requirements for CO2 fixation of NH4+ assimilation in this organism. When grown under N-sufficient conditions, NH4+ assimilation is directly dependent upon photosynthetic CO2 fixation to provide carbon skeletons for amino acid synthesis. When cultured under N-limited conditions, the cells accumulate starch, which is then available for amino acid synthesis. This alleviates the requirement of photosynthetic CO2 fixation for NH4+ assimilation. N-limited cells, however, still exhibit a nonphotosynthetic CO2 requirement for N assimilation that is mediated through PEPC. This activity of PEPC increases during N assimilation to replenish TCA cycle intermediates consumed during amino acid synthesis. The in vivo activity of this enzyme is tightly regulated so that there are ~0.3 moles C fixed per mole N assimilated. In S. minutum PEPC is regulated primarily by the ratio of glutamine/glutamate, thus providing a mechanism by which primary NH4+ assimilation modulates the supply of carbon for amino acid biosynthesis. Activation of PEPC during NH4+ assimilation occurs in both the light and the dark. Key words: dissolved inorganic carbon, nitrogen assimilation, phosphoenolpyruvate carboxylase, photosynthesis, amino acid synthesis, respiration.

scholarly journals Arabidopsis thaliana contains two phosphoenolpyruvate carboxylase kinase genes with different expression patterns

2002 ◽  
Vol 25 (1) ◽  
pp. 115-122 ◽  
Author(s):  
V. Fontaine ◽  
J. Hartwell ◽  
G. I. Jenkins ◽  
H. G. Nimmo
Keyword(s):  
Arabidopsis Thaliana ◽  
Phosphoenolpyruvate Carboxylase ◽  
Expression Patterns ◽  
Phosphoenolpyruvate Carboxylase Kinase

In-situ evidence for the involvement of calcium and bundle-sheath-derived photosynthetic metabolites in the C4 phosphoenolpyruvate-carboxylase kinase signal-transduction chain

Planta ◽  
1996 ◽  
Vol 199 (3) ◽  
Author(s):  
StephenM.G. Duff ◽  
Nathalie Giglioli-Guivarc'h ◽  
Jean-No�l Pierre ◽  
Jean Vidal ◽  
ShirleyA. Condon ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Phosphoenolpyruvate Carboxylase ◽  
Bundle Sheath ◽  
Phosphoenolpyruvate Carboxylase Kinase

scholarly journals pH and carbon supply control the expression of phosphoenolpyruvate carboxylase kinase genes inArabidopsis thaliana

2008 ◽  
Vol 31 (12) ◽  
pp. 1844-1850 ◽  
Author(s):  
ZHI-HUI CHEN ◽  
GARETH I. JENKINS ◽  
HUGH G. NIMMO
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Carbon Supply ◽  
Phosphoenolpyruvate Carboxylase Kinase

scholarly journals The light induction of maize phosphoenolpyruvate carboxylase kinase translatable mRNA requires transcription but not translation

1999 ◽  
Vol 22 (7) ◽  
pp. 883-889 ◽  
Author(s):  
J. Hartwell ◽  
G. I. Jenkins ◽  
M. B. Wilkins ◽  
H. G. Nimmo
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Light Induction ◽  
Phosphoenolpyruvate Carboxylase Kinase ◽  
Translatable Mrna
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