Transcriptional regulation of the ADP-glucose pyrophosphorylase isoforms in the leaf and the stem under long and short photoperiod in lentil

Seferoglu, Ayse Bengisu; Barış, İbrahim; Morgil, Hande; Tulum, Isil; Ozdas, Sule; Cevahir, Gül; Kavaklı, İbrahim Halil

doi:10.1016/j.plantsci.2013.01.006

Cited by 12 publications

(9 citation statements)

References 60 publications

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“…Chen et al reported that AGPase activity in the leaves of rice seedlings slightly decreased under salt stress (Chen et al, 2008 ). Several studies discussed AGPase activity in the stems, which is important in the pooling of carbohydrates (Cook et al, 2012 ; Seferoglu et al, 2013 ), but upregulation of AGPase in the stems by mineral stress has not been reported. Whether Cd directly regulates enzymes involved in carbohydrate metabolism or indirectly influences carbon metabolism requires further study.…”

Section: Discussionmentioning

confidence: 99%

Common reed accumulates starch in its stem by metabolic adaptation under Cd stress conditions

et al. 2015

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In a previous study, we reported that the common reed accumulates water-soluble Cd complexed with an α-glucan-like molecule, and that the synthesis of this molecule is induced in the stem of the common reed under Cd stress. We studied the metabolic background to ensure α-glucan accumulation under the Cd stress conditions that generally inhibit photosynthesis. We found that the common reed maintained an adequate CO2 assimilation rate, tended to allocate more assimilated 11C to the stem, and accumulated starch granules in its stem under Cd stress conditions. AGPase activity, which is the rate-limiting enzyme for starch synthesis, increased in the stem of common reed grown in the presence of Cd. Starch accumulation in the stem of common reed was not obvious under other excess metal conditions. Common reed may preferentially allocate assimilated carbon as the carbon source for the formation of Cd and α-glucan complexes in its stem followed by prevention of Cd transfer to leaves acting as the photosynthetic organ. These responses may allow the common reed to grow even under severe Cd stress conditions.

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Section: Discussionmentioning

confidence: 99%

Common reed accumulates starch in its stem by metabolic adaptation under Cd stress conditions

et al. 2015

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“…Different AGPase isoforms respond differently to photoperiod, circadian clock or sugar (Geigenberger 2011;Seferoglu et al 2013). The Arabidopsis genes APL3 and APL4 are induced by both Suc and hexoses in leaves (Li et al 2002;Thellin et al 2009;Michalska et al 2009).…”

Section: Transitory Starch Is Highly Responsive To the External Envirmentioning

confidence: 99%

“…The Arabidopsis genes APL3 and APL4 are induced by both Suc and hexoses in leaves (Li et al 2002;Thellin et al 2009;Michalska et al 2009). In lentil leaves, some AGPase isoforms are differentially regulated during short and long days (Seferoglu et al 2013). Overall, it can be said that the expression of isogenes is certainly tissuedependent, such as in the case of AGPase (Huang et al 2014).…”

Section: Transitory Starch Is Highly Responsive To the External Envirmentioning

confidence: 99%

Peer Review #2 of "Exploring regulatory networks in plants: transcription factors of starch metabolism (v0.1)"

Szydlowski¹

2019

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Biological networks are complex (non-linear), redundant (cyclic) and compartmentalized at the subcellular level. Rational manipulation of plant metabolism may have failed due to inherent difficulties of a comprehensive understanding of regulatory loops. We first need to identify key factors controlling the regulatory loops of primary metabolism. The paradigms of plant networks are revised in order to highlight the differences between metabolic and transcriptional networks. Comparison between animal and plant transcription factors (TFs) reveal some important differences. Plant transcriptional networks function at a lower hierarchy compared to animal regulatory networks. Plant genomes contain more TFs than animal genomes, but plant proteins are smaller and have less domains as animal proteins which are often multifunctional. We briefly summarize mutant analysis and co-expression results pinpointing some TFs regulating starch enzymes in plants. Detailed information is provided about biochemical reactions, TFs and cis regulatory motifs involved in sucrose-starch metabolism, in both source and sink tissues. Examples about coordinated responses to hormones and environmental cues in different tissues and species are listed. Further advancements require combined data from single-cell transcriptomic and metabolomic approaches. Cell fractionation and subcellular inspection may provide valuable insights. We propose that shuffling of promotorpromoter elements might be a promising strategy to improve in the near future starch content, crop yield or food quality.

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“…When the OD 600 of the culture was reached 1.0, the cells were induced with 0.1 mM IPTG, and the protein expression was induced for 18 h at room temperature. The cells were harvested and disrupted by sonication in 25 ml of binding buffer (25 mM HEPES-NaOH, pH8.0, 5% glycerol) supplemented with 0.5 mg/L lysozyme, EDTA-free protease inhibitor cocktail (Sigma), and 1 mM PMSF [40]. The soluble fraction was separated by centrifugation and passed through Macroprep DEAE resin (BIORAD).…”

Section: His-tagged Protein Expression and Purificationmentioning

confidence: 99%

Glu-370 in the Large Subunit Influences the Substrate Binding, Allosteric, and Heat Stability Properties of Potato ADP-glucose Pyrophosphorylase

Seferoglu

Gül

Dikbas

et al. 2016

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ADP-glucose pyrophosphorylase (AGPase) is a key allosteric enzyme in plant starch biosynthesis. Plant AGPase is a heterotetrameric enzyme that consists of large (LS) and small subunits (SS), which are encoded by two different genes. In this study, we showed that the conversion of Glu to Gly at position 370 in the LS of AGPase alters the heterotetrameric stability along with the binding properties of substrate and effectors of the enzyme. Kinetic analyses revealed that the affinity of the LS E370G SS WT AGPase for glucose-1-phosphate is 3-fold less than for wild type (WT) AGPase. Additionally, the LS E370G SS WT AGPase requires 3-fold more 3-phosphogyceric acid to be activated. Finally, the LS E370G SS WT AGPase is less heat stable compared with the WT AGPase.Computational analysis of the mutant Gly-370 in the 3D modeled LS AGPase showed that this residue changes charge distribution of the surface and thus affect stability of the LS AGPase and overall heat stability of the heterotetrameric AGPase. In summary, our results show that LS E370 intricately modulate the heat stability and enzymatic activity of the AGPase.

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Transcriptional regulation of the ADP-glucose pyrophosphorylase isoforms in the leaf and the stem under long and short photoperiod in lentil

Cited by 12 publications

References 60 publications

Common reed accumulates starch in its stem by metabolic adaptation under Cd stress conditions

Common reed accumulates starch in its stem by metabolic adaptation under Cd stress conditions

Peer Review #2 of "Exploring regulatory networks in plants: transcription factors of starch metabolism (v0.1)"

Glu-370 in the Large Subunit Influences the Substrate Binding, Allosteric, and Heat Stability Properties of Potato ADP-glucose Pyrophosphorylase

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