Cloning and characterization of ADP-glucose pyrophosphorylase small subunit gene in Cyperus esculentus (yellow nutsedge)

Abstract

ABSTRACT. ADP-glucose pyrophosphorylase (ADPGlcPPase) controls the first committed step of starch synthesis by catalyzing the biosynthesis of ADP-glucose from glucose-phosphate and ATP. It is a tetrameric protein consisting of two small and two large subunits. The small subunits have a catalytic function, while the large subunits regulate the enzyme activity. Cyperus esculentus (yellow nutsedge) is a perennial C 4 plant grown from rhizomes and tubers. Previous studies on yellow nutsedge have mostly focused on the morphology and cultivation of tubers, their application in food, and biochemical analyses of the tubers. In this study, the gene encoding the ADPGlcPPase small subunit (CeAGPS) in yellow nutsedge was cloned and characterized. The full-length CeAGPS cDNA sequence contained an 81-bp 5'-untranslated region (UTR), a 188-bp 3'-UTR, and a 1539-bp open reading frame encoding 512-amino acid residues. The genomic sequence of CeAGPS comprises a nine exon-eight intron structure similar to the previously reported cotton and Arabidopsis thaliana AGPS 18303©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 14 (4): 18302-18314 (2015) Cloning and characterization of AGPS in yellow nutsedge genes. The deduced translation product of the CeAGPS gene contained a well-conserved catalytic domain and regulatory elements typical of plant AGPS. Reverse transcriptase polymerase chain reaction amplification of the target gene in various plant parts using gene-specific primers indicated that the expression of CeAGPS was most abundant in the tuber, and relatively lower in nutsedge roots.

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“…The yellow nutsedge tubers were germinated at 22 °C under a 16 h light/8 h dark cycle. RNA was isolated from leaves, roots and fresh tubers as described by Cheng et al [ 63 ].…”

Tiger nut (Cyperus esculentus) starch: extraction, composition, structure, properties, modification and uses

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Comparative transcriptome analysis indicates conversion of stamens into pistil-like structures in male sterile wheat (Triticum aestivum L.) with Aegilops crassa cytoplasm

“…In monocots, AGPase comprises two large subunits and two small subunits, which interact and polymerize into the native heterotetrameric enzyme structure [21,22]. The small subunit is the catalytic center of the enzyme and the key site for enzyme allosteric effects [23]. The two subunits are encoded by different genes and studies of Arabidopsis have shown that they are functionally interdependent.…”