Molecular Cloning and Expression Analysis of the Starch-branching Enzyme III Gene from Common Wheat (Triticum aestivum )

Kang, Guozhang; Li, Shuyi; Zhang, Mengqin; Peng, Huifang; Wang, Chenyang; Zhu, Yunji; Guo, Tao

doi:10.1007/s10528-013-9570-4

Cited by 18 publications

(14 citation statements)

References 17 publications

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“…Many previous studies have reported enzymes that are directly involved in starch biosynthesis in algae 14 , potato 15 , Arabidopsis thaliana 16 , barley 17 , wheat 18 , 19 , and rice 20 , 21 . However, far less research has been devoted to the core regulatory network involved in starch metabolism.…”

Section: Introductionmentioning

confidence: 99%

Evolutionary, structural and expression analysis of core genes involved in starch synthesis

Zhang

et al. 2018

Sci Rep

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Starch is the main storage carbohydrate in plants and an important natural resource for food, feed and industrial raw materials. However, the details regarding the pathway for starch biosynthesis and the diversity of biosynthetic enzymes involved in this process are poorly understood. This study uses a comprehensive phylogenetic analysis of 74 sequenced plant genomes to revisit the evolutionary history of the genes encoding ADP-glucose pyrophosphorylase (AGPase), starch synthase (SS), starch branching enzyme (SBE) and starch de-branching enzyme (DBE). Additionally, the protein structures and expression patterns of these four core genes in starch biosynthesis were studied to determine their functional differences. The results showed that AGPase, SS, SBE and DBE have undergone complicated evolutionary processes in plants and that gene/genome duplications are responsible for the observed differences in isoform numbers. A structure analysis of these proteins suggested that the deletion/mutation of amino acids in some active sites resulted in not only structural variation but also sub-functionalization or neo-functionalization. Expression profiling indicated that AGPase-, SS-, SBE- and DBE-encoding genes exhibit spatio-temporally divergent expression patterns related to the composition of functional complexes in starch biosynthesis. This study provides a comprehensive atlas of the starch biosynthetic pathway, and these data should support future studies aimed at increasing understanding of starch biosynthesis and the functional evolutionary divergence of AGPase, SS, SBE, and DBE in plants.

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Section: Introductionmentioning

confidence: 99%

Evolutionary, structural and expression analysis of core genes involved in starch synthesis

Zhang

et al. 2018

Sci Rep

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“…SBEI belonged to family B, which has been reported in a range of species. and SBEIII belonged to family A, which has only been identified in maize, wheat, rice and lotus, and little research has been done about this isoform (Kang et al 2013;Tian et al 2009).…”

Section: Discussionmentioning

confidence: 99%

Genetic diversity, functional properties and expression analysis of NnSBE genes involved in starch synthesis of lotus (Nelumbo nucifera Gaertn.)

Zhu

Sun

Diao

et al. 2019

Preprint

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Background. Starch branching enzyme (SBE) is one of the key enzymes in starch biosynthetic metabolism and determines the structure of amylopectin. Methods. Full length of SBE genes were cloned by reverse transcription PCR (RT-PCR) technology, and used neighbor-joining (NJ) tree for phylogenetic analysis. The single nucleotide polymorphisms (SNPs) were determined to assess the genetic polymorphisms and variation indexes between individuals and clusters. Quantitative real time PCR (qRT-PCR) was performed to analyse spatial and temporal expression of SBE genes. Effect of NnSBE genes on fine structure of amylopectin was explore by affinity and enzyme activity analysis of two isoforms in amylopectin and amylose. Results. In this study, two SBE family genes, NnSBEI and NnSBEIII were identified from lotus (Nelumbo nucifera Gaertn.). Phylogenetic analysis divided the NnSBEI into SBE family B and NnSBEIII was belong to SBE family A. The homozygous haplotype (AA GG GG AA GG) of NnSBEIII was observed in seed lotus. During the seed embryo development stage, NnSBEIII reached the peak in middle of development stage and while NnSBEI increased in mid-late developmental stage. The different affinity activity of two isozymes bind amylopectin and amylose assay indicated NnSBEI has higher activity and wider affinity. Discussion. This study showed that NnSBE genes received artificial selection during the process of cultivation and domestication in seed lotus especially. Furthermore, the expression pattern and affinity activity analysis indicated that NnSBE genes was related to chain length of amylopectin.

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“…In Arabidopsis, deficiency in BEIII was reported not to influence the structure of starch (42), but BEIII was shown to be essential for embryogenesis (43). Nevertheless, it has been reported that the recombinant form of BEIII from wheat (Triticum aestivum) exhibits branching activity (44). No other studies on the characterization of BEIII have been described, except for the above-mentioned reports.…”

Section: Gh13_8 Be Consists Of At Least Three Domains As Followsmentioning

confidence: 99%

Structure and Function of Branching Enzymes in Eukaryotes

Suzuki

2020

TIGG

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Brancihing enzymes (BEs) catalyze the transglycosylation reactions to form a new branching point consisting of an α-1,6glucosidic linkage by cleaving an α-1,4-glucosidic linkage of an α-glucan chain. BEs are ubiquitous throughout the prokaryotes but are only found in limited taxa in the eukaryotes. Prokaryotic and eukaryotic BEs are classified into distinct families based on similarities in their primary structures. Land plants have multiple BE isoforms, whose function in vivo has been identified using mutants. Recent studies have revealed that plant BEs form protein-protein complexes with related enzymes involved in α-glucan metabolism in vivo. Although their biological significance is unclear, it is proposed that they are essential for efficient amylopectin biosynthesis. Crystal structures of BEs from eukaryotes (rice and human) are now available. These two structures have the same domain organization, containing a catalytic domain common to all members of glycoside hydrolase family 13. Recently, the authors have reported the structures of BE from a cyanobacterium (a photosynthetic prokaryote) in complex with maltooligosaccharides at the active site. On the other hand, little is known about the structure-function relationship of eukaryotic BEs. This review describes recent progress in research on the structure and function of eukaryotic BEs. A. Introduction Haworth et al. isolated an enzyme preparation from potato and discovered enzymatic activity that produced amylopectin-like branched glucan from amylose; this enzyme was named the Qenzyme (1), but the group of enzymes is now generally called the branching enzymes (BEs; EC 2.4.1.18). The transglycosylation reaction catalyzed by BE is accomplished by cleavage of an α-1,4glucosidic bond of the donor substrate and transfer of the glucan chain to the acceptor substrate to form a new branching point composed of an α-1,6-glucosidic linkage. It has been suggested that, in this reaction, both inter-and intramolecular transglycosylation is possible (Fig. 1) (2, 3). Starch and glycogen are α-glucans composed solely of glucose units, but they differ in terms of their structure and properties. Amylopectin, the main component of starch, has a repetitive structure (referred to as a tandem-cluster structure) consisting of regions with high (amorphous lamellae) and low branch frequency (crystalline lamellae) (Fig. 2, left panel). The structure makes the amylopectin to become insoluble, and thus amylopectin displays crystallinity, gelatinization, and paste viscosity. In contrast, randomly branched glycogen has high water solubility and does not display properties like amylopectin (Fig. 2, right panel). The branching structures of the glucans determine their properties (4, 5). BEs play key roles in α-glucan biosynthesis by determining the branching patterns of α-glucans (3, 5-7). BEs are distributed among prokaryotes and some eukary-MINIREVIEW

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Molecular Cloning and Expression Analysis of the Starch-branching Enzyme III Gene from Common Wheat (Triticum aestivum )

Cited by 18 publications

References 17 publications

Evolutionary, structural and expression analysis of core genes involved in starch synthesis

Evolutionary, structural and expression analysis of core genes involved in starch synthesis

Genetic diversity, functional properties and expression analysis of NnSBE genes involved in starch synthesis of lotus (Nelumbo nucifera Gaertn.)

Structure and Function of Branching Enzymes in Eukaryotes

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