Protein and gene expression characteristics of a rice phosphoenolpyruvate carboxylase Osppc3; its unique role for seed cell maturation

Yamamoto, Nobuto; Sasou, Ai; Saito, Yuhi; Sugimoto, Tsuneaki; Masumura, Takehiro

doi:10.1016/j.jcs.2015.04.008

Cited by 9 publications

(8 citation statements)

References 27 publications

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“…This result indicates that plant-type isoforms should be more abundant than bacterial-type isoforms. In accordance with this assumption, our reverse transcription-polymerase chain reaction analysis in rice failed to detect any expression of the bacterial-type PEPC Osppc-b (Yamamoto et al 2015). Smaller amounts of bacterial-type PEPC might be expressed in the developing seeds of cereals.…”

Section: Expression Of Pepc Proteinsupporting

confidence: 75%

“…PEPC is involved in various kinds of primary metabolism: e.g., C4 photosynthesis, respiration and nitrogen assimilation (O'Leary et al 2011). PEPC also plays a key role in seed maturation by providing precursors for amino acid and fatty acid biosynthesis; oxaloacetate is converted into aspartate by aspartate aminotransferase or malate, which is an important intermediate for lipid biosynthesis, by malate dehydrogenase (Rolletschek et al 2004;O'Leary et al 2011;Fan et al 2013;Yamamoto et al 2015). High-level PEPC activity in developing seeds suggests the physiological importance of this enzyme for CONTACT Takehiro Masumura masumura@kpu.ac.jp seed formation (Sangwan et al 1992;Sugimoto et al 1998;Yamamoto et al 2014a).…”

Section: Introductionmentioning

confidence: 99%

“…In common wheat, PEPC activity seems to be regulated by nitrogen incorporation into seeds from source organs (Zhang et al 2012;Yamamoto et al 2014c). At the cellular level, the cereal PEPC protein was substantially localized in the aleurone layer and in embryonic cells at the grain-filling stage (González et al 1998;Yamamoto et al 2015). Araus et al (1993) reported the subcellular localization of PEPC in phytate globoids in durum wheat, in which the organelle stores seed storage protein globulins.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, different characteristics of PEPC isogenes have been found; for example, a rice PEPC, Osppc1, which is categorized as a plant-type PEPC (Masumoto et al 2010), was isolated from developing rice seeds as a main isogene, and it showed distinctive enzymatic properties in comparison with other PEPCs (Yamamoto et al 2014a;Muramatsu et al 2015). In contrast, the plant-type PEPC Osppc3 plays a role in fatty acid biosynthesis in developing rice seeds (Yamamoto et al 2015). These findings suggest the presence of functional partitioning of PEPC isogenes in primary metabolism.…”

Section: Introductionmentioning

confidence: 99%

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Role of nitrogen-responsive plant-type phosphoenolpyruvate carboxylase in the accumulation of seed storage protein in ancient wheat (spelt and kamut)

Yamamoto

Kinoshita

Sugimoto

et al. 2017

Soil Science and Plant Nutrition

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Ancient wheat such as Triticum spelta L. and T. turanicum is a possible genetic material for improving wheat seed quality due to its grain characteristics, which differ from those of common wheat. Ancient wheat grains accumulate proteins with fewer allergens and higher levels of essential amino acids, antioxidants, minerals and vitamins. The identification of a genetic factor that controls seed protein content would be useful for breeding wheat varieties in accordance with various purposes. Previous studies implied that phosphoenolpyruvate carboxylase (PEPC) is involved in nitrogen accumulation in crop seeds. However, multiple types of PEPC genes are present in plant genomes, and it has still not been clarified yet which type of PEPC is relevant to seed nitrogen metabolism. In this study, to determine which PEPC is involved in seed protein accumulation in ancient wheat, we examined the effects of different levels of nitrogen application at the flowering stage on PEPC activity on developing seeds and on the protein content in mature seeds of three ancient wheat varieties. The responses of the PEPC activity and seed protein content were observed, but their patterns differed among the varieties. Among the experimental plots, PEPC activity and seed protein content showed a high correlation (r = 0.757, p value = 1.09E −3). Immunoblot analysis revealed that plant-type PEPC seemed to underlie the response of PEPC activity to nitrogen application, while no bacterial-type PEPC was detected by a peptide-antigen antibody. These results indicate that plant-type PEPC plays an important role in storage protein accumulation in ancient wheat seeds under nitrogen application at the flowering stage.

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Section: Expression Of Pepc Proteinsupporting

confidence: 75%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Role of nitrogen-responsive plant-type phosphoenolpyruvate carboxylase in the accumulation of seed storage protein in ancient wheat (spelt and kamut)

Yamamoto

Kinoshita

Sugimoto

et al. 2017

Soil Science and Plant Nutrition

Self Cite

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“…Plant PEPC is a key enzyme in photosynthesis, seed development [ 19 , 20 , 21 , 22 , 23 ], nutrient accumulation and metabolism [ 16 , 24 , 25 ], and abiotic stress adaptation [ 1 , 26 , 27 , 28 , 29 ]. One of the important seed crops, peanut, has five PEPC genes that can regulate the metabolic process of fatty acid and protein biosynthesis in seeds [ 16 ].…”

Section: Discussionmentioning

confidence: 99%

Prokaryotic Expression of Phosphoenolpyruvate Carboxylase Fragments from Peanut and Analysis of Osmotic Stress Tolerance of Recombinant Strains

Feng

Hong

et al. 2021

Plants

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Phosphoenolpyruvate carboxylase (PEPC) is a ubiquitous cytosolic enzyme that catalyzes the irreversible β-carboxylation of phosphoenolpyruvate (PEP) in presence of HCO3− to produce oxaloacetate (OAA) during carbon fixation and photosynthesis. It is well accepted that PEPC genes are expressed in plants upon stress. PEPC also supports the biosynthesis of biocompatible osmolytes in many plant species under osmotic stress. There are five isoforms of PEPC found in peanut (Arachis hypogaea L.), namely, AhPEPC1, AhPEPC2, AhPEPC3, AhPEPC4, and AhPEPC5. Quantitative real-time polymerase chain reaction (qRT-PCR) analysis revealed that the gene expression patterns of these AhPEPC genes were different in mature seeds, stems, roots, flowers, and leaves. The expression of all the plant type PEPC (PTPCs) (AhPEPC1, AhPEPC2, AhPEPC3, and AhPEPC4) was relatively high in roots, while the bacterial type PEPC (BTPC) (AhPEPC5) showed a remarkable expression level in flowers. Principal component analysis (PCA) result showed that AhPEPC3 and AhPEPC4 are correlated with each other, indicating comparatively associations with roots, and AhPEPC5 have a very close relationship with flowers. In order to investigate the function of these AhPEPCs, the fragments of these five AhPEPC cDNA were cloned and expressed in Escherichia coli (E. coli). The recombinant proteins contained a conserved domain with a histidine site, which is important for enzyme catalysis. Results showed that protein fragments of AhPEPC1, AhPEPC2, and AhPEPC5 had remarkable expression levels in E. coli. These three recombinant strains were more sensitive at pH 9.0, and recombinant strains carrying AhPEPC2 and AhPEPC5 fragments exhibited more growth than the control strain with the presence of PEG6000. Our findings showed that the expression of the AhPEPC fragments may enhance the resistance of transformed E. coli to osmotic stress.

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Rapidly evolving phosphoenolpyruvate carboxylase Gmppc1 and Gmppc7 are highly expressed in the external seed coat of immature soybean seeds

Yamamoto

Takano

Masumura

et al. 2020

Gene

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Protein and gene expression characteristics of a rice phosphoenolpyruvate carboxylase Osppc3; its unique role for seed cell maturation

Cited by 9 publications

References 27 publications

Role of nitrogen-responsive plant-type phosphoenolpyruvate carboxylase in the accumulation of seed storage protein in ancient wheat (spelt and kamut)

Role of nitrogen-responsive plant-type phosphoenolpyruvate carboxylase in the accumulation of seed storage protein in ancient wheat (spelt and kamut)

Prokaryotic Expression of Phosphoenolpyruvate Carboxylase Fragments from Peanut and Analysis of Osmotic Stress Tolerance of Recombinant Strains

Rapidly evolving phosphoenolpyruvate carboxylase Gmppc1 and Gmppc7 are highly expressed in the external seed coat of immature soybean seeds

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