Molecular Cloning and Characterization of a cDNA Encoding Putative Phospholipid Hydroperoxide Glutathione Peroxidase from Spinach

Sugimoto, Mineharu; Furui, Satoshi; Suzuki, Yukio

doi:10.1271/bbb.61.1379

Cited by 45 publications

(30 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The polypeptide encoded by this ORF has an Mr value of 105,400 and an isoelectric point of 5.75. The most significant similarity matches of this amino acid sequence were with members of family 31 of glucosyl transferases (Henrissat and Bairoch, 1993) which includes α-glucosidases from barley (Tibbot and Skadsen, 1996), spinach (Sugimoto et al, 1997), humans (Hoefsloot et al, 1988) and Candida tsukubaenis (Kinsella et al, 1991). The most similar full-length sequences were those of the barley and human α-glucosidases with an overall similarity of approximately 50% and identity of 29%.…”

Section: Resultsmentioning

confidence: 86%

“…For example, isoforms I and II from spinach (Sugimoto et al, 1997), and the low pI isoform from barley (Sun and Henson, 1990), both use starch as well as a range of malto-oligosaccharides as substrates, whereas isoforms III and IV from spinach and the high pI isoform from barley only catalyse the hydrolysis of maltooligosaccharides. The extent to which the different isoforms are encoded by different gene families or are produced as a result of differential post-translational modification remains to be determined.…”

Section: Introductionmentioning

confidence: 99%

“…The extent to which the different isoforms are encoded by different gene families or are produced as a result of differential post-translational modification remains to be determined. In spinach, four isoforms are probably derived from differential post-translational modification of one precursor gene product (Sugimoto et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

“…These include those describing a cDNA clone of a putative GA-inducible barley α-glucosidase (Tibbot and Skadsen, 1996), a cDNA clone of an α-glucosidase gene from spinach (Sugimoto et al, 1997), and an Arabidopsis expressed sequence tag (EST) that has sequence similarity to Candida tsukubaenis and human lysosomal α-glucosidase genes (Newman et al, 1994). In this study, the Arabidopsis EST was used as a probe to isolate a corresponding full length cDNA from a developing potato tuber cDNA library.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

cDNA cloning and characterisation of an α‐glucosidase gene from potato (Solanum tuberosum L.)

Taylor¹,

George²,

Ross³

et al. 1998

The Plant Journal

View full text Add to dashboard Cite

SummaryUsing an Arabidopsis thaliana expressed sequence tag with sequence similarity to human lysosomal α-glucosidase as a probe, a potato cDNA was isolated. The cDNA encodes a polypeptide with an Mr value of 105,400 and the most significant matches of the deduced amino acid sequence are with members of family 31 of glucosyl transferase. The potato cDNA was expressed in a strain of Saccharomyces cerevisiae that is deficient in maltase activity and unable to grow using maltose as a carbon source (ABYSMAL81). Expression of the potato cDNA in the mutant yeast strain restores its ability to use maltose as a carbon source for growth. Additionally, α-glucosidase activity could be measured in extracts of the yeast cells following complementation. A range of maltodextrins were substrates for this activity. The steady-state expression level of the potato α-glucosidase gene was low in most tissues examined, the highest levels occurring in sprouting tubers and source leaves.

show abstract

Section: Resultsmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

cDNA cloning and characterisation of an α‐glucosidase gene from potato (Solanum tuberosum L.)

Taylor¹,

George²,

Ross³

et al. 1998

The Plant Journal

View full text Add to dashboard Cite

show abstract

“…Asterisks show the aromatic amino acid residues replaced by alanine. OAG1, rice (Oryza sativa L., var Akamai) α glucosidase 1 (E792 Y906); BAG, barley high pI α glucosidase (E768 Y879); 15) SNG, spinach α glucosidase (V795 H903); 16) SBG, sugar beet α glucosidase (I799 R913); 17) ATG, Arabidopsis thaliana α glucosidase (E789 T902); 18) ANG, A. niger α glucosidase (E894 N980); 19,20) SPG, S. pombe α glucosidase (V880 L969); 21) SOG, S. occidentalis α glucosidase (E874 W960). 13,14) Trp885 in chimeric enzyme (Trp803 in rice α glucosidase) was associated with the hydrolysis of longer chain substrates as well as the attack on starch granules.…”

mentioning

confidence: 99%

Plant .ALPHA.-Glucosidase: Molecular Analysis of Rice .ALPHA.-Glucosidase and Degradation Mechanism of Starch Granules in Germination Stage

博之¹,

達也²,

茂紀³

et al. 2006

J. Appl. Glycosci.

View full text Add to dashboard Cite

Starch is an abundant carbohydrate widespread in plants. This high energy polysaccharide is preserved in the storage tissues, such as seeds. In the germination of plant seeds, the starch is degraded by several hydrolytic enzymes (α amylase, β amylase, debranching enzyme and α glucosidase), followed by conversion to the biological materials and energy necessary for growth. 1) In plant seeds, starch exists as practically insoluble polysaccharide called starch granules or raw starch. Therefore, the pathway of starch degradation in the germination stage has been generally considered as follows. 2)α Amylase is a key enzyme attacking the starch granules initially to liberate soluble dextrin. Produced dextrin is hydrolyzed by the further action combined with α amylase, β amylase and debranching enzyme to form oligosaccharides such as maltose. Finally, α glucosidase converts the oligosaccharides to glucose. Among these starch degrading enzymes α amylase has been considered to be the exclusive enzyme capable of hydrolyzing the starch granules, while the other enzymes were not. However, it had been reported that plant α glucosidases exhibited the ability to attack soluble starch effectively, 3,4) which suggested that α glucosidase hydrolyzed not only oligosaccharides such as maltose but starch as well in plant seeds. Recently, barley, 5,6) millet 7,8) and rice 9,10) α glucosidases were found to be capable of degrading the starch granules. The combination of α glucosidase and α amylase exhibited the synergism of degradation of starch granules. 5,6,11) It is of interest to learn the α glucosidase mediated starch metabolism in the germination stage. The first section of this article introduces our molecular level analysis on the degradation of starch granules catalyzed by plant α glucosidase.In the second section, we describe the multiple formation mechanism of rice α glucosidases observed in the ripening and germination stages. α Glucosidases, which are synthesized in the ripening stage and preserved in dry seeds, are important in starch metabolism, since these enzymes hydrolyze starch granules before attacking by α amylase. Certain α glucosidase isozymes, which are expressed in the early stage of germination, also hydrolyze starch granules. It is valuable to learn the expression systems of α glucosidases in the dry seeds and germinating seeds. In both seeds, there were several enzymes, of which the expression feature differed by variety of rice, requiring more precise analysis to understand the contribution of each enzyme to starch metabolism. The second section of this article introduces the mechanism for the formation of rice α glucosidase isoforms and isozymes as well as their characteristics elucidated using purified en- Abstract: In germination of plant seeds, storage starch is principally degraded by the combination of amylolytic enzymes. As starch is an insoluble granule, a conventional view of the degradation pathway is that the initial attack is performed by α-amylase having the starch granule-binding ability. Pla...

show abstract

IDENTIFICATION AND CHARACTERIZATION OF TWO PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE GENES FROM THE MEDITERRANEAN SPECIES OF THE WHITEFLY Bemisia tabaci COMPLEX

Jiu

Xianlong

et al. 2015

Arch Insect Biochem Physiol

View full text Add to dashboard Cite

Phospholipid hydroperoxide glutathione peroxidases (PHGPXs) are essential enzymes of the cellular antioxidant defense system during insect-plant interactions. However, little attention has been devoted to the functional characterization of PHGXPs in the whitefly Bemisia tabaci. Here, we report the identification and characterization of two PHGPX genes, designated as BtQ-PHGPX1 and BtQ-PHGPX2 from the Mediterranean species of the B. tabaci complex. Sequence analysis indicated that the length of BtQ-PHGPX1 is of 942 bp with a 729 bp open-reading frame (ORF) encoding 242 amino acids, and BtQ-PHGPX2 is of 699 bp with a 567 bp ORF encoding 188 amino acids. Sequence alignment analysis showed that BtQ-PHGPX1 and BtQ-PHGPX2 shared high similarity with other known PHGPXs. The NVASXCGXT, FPCNQFXXQEPG, and IKWNFXKFLV surrounded the reactive cysteine, glutamine, and tryptophan residues, respectively. Recombinant BtQ-PHGPX1 and BtQ-PHGPX2 were overexpressed in Escherichia coli and purified. quantitative reverse transcription-polymerase chain reaction (qRT-PCR) analysis with whiteflies of different development stages showed that the mRNA levels of BtQ-PHGPX2 were significantly higher in larvae than in other stages. The mRNA levels of BtQ-PHGPX2 were significantly higher than BtQ-PHGPX1 during all the developmental stages. The mRNA levels of BtQ-PHGPX1 and BtQ-PHGPX2 in female adults were relatively higher than in male adults. The expression of BtQ-PHGPX1 and BtQ-PHGPX2 was induced by the insecticide imidacloprid. These results suggest that BtQ-PHGPX1 and BtQ-PHGPX2 may participate in detoxification of oxidative hazards in B. tabaci.

show abstract

Molecular Cloning and Characterization of a cDNA Encoding Putative Phospholipid Hydroperoxide Glutathione Peroxidase from Spinach

Cited by 45 publications

References 5 publications

cDNA cloning and characterisation of an α‐glucosidase gene from potato (Solanum tuberosum L.)

cDNA cloning and characterisation of an α‐glucosidase gene from potato (Solanum tuberosum L.)

Plant .ALPHA.-Glucosidase: Molecular Analysis of Rice .ALPHA.-Glucosidase and Degradation Mechanism of Starch Granules in Germination Stage

IDENTIFICATION AND CHARACTERIZATION OF TWO PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE GENES FROM THE MEDITERRANEAN SPECIES OF THE WHITEFLY Bemisia tabaci COMPLEX

Contact Info

Product

Resources

About