Abstract

Two genes encoding putative glutathione S-transferase proteins were isolated from pear (Pyrus pyrifolia) and designated PpGST1 and PpGST2. The deduced PpGST1 and PpGST2 proteins contain conserved Glutathione S-transferase N-terminal domain (GST_N) and Glutathione S-transferase, C-terminal domain (GST_C). Using PCR amplification technique, the genomic clones corresponding to PpGST1 and PpGST2 were isolated and shown to contain two introns and a singal intron respectively with typical GT/AG boundaries defining the splice junctions. Phylogenetic analysis clearly demonstrated that PpGST1 belonged to Phi class of GST superfamilies and had high homology with apple MdGST, while PpGST2 was classified into the Tau class of GST superfamilies. The expression of PpGST1 and PpGST2 genes was developmentally regulated in fruit. Further study demonstrated that PpGST1 and PpGST2 expression was remarkably induced by glucose, salicylic acid (SA) and indole-3-aceticacid (IAA) treatments in pear fruit, and in diseased fruit. These data suggested that PpGST1 and PpGST2 might be involved in response to sugar, SA, and IAA signaling during fruit development of pear.

Highlights

  • Glutathione S-transferases (GSTs; EC 2.5.1.18) are a superfamily of multifunctional enzymes that catalyze the nucleophilic conjugation of reduced tripeptide glutathione (GSH; g-Glu-CysGly) into a variety of hydrophobic and electrophilic compounds to direct them to specific sites both intra- and extracellularly

  • The isolated cDNAs were designated as PpGST1 and PpGST2, accession numbers in GenBank: KF730655 and KF730656

  • Compared with its cDNA sequence, we found that PpGST1 gene contains two introns in its open reading frame (ORF)

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Summary

Introduction

Glutathione S-transferases (GSTs; EC 2.5.1.18) are a superfamily of multifunctional enzymes that catalyze the nucleophilic conjugation of reduced tripeptide glutathione (GSH; g-Glu-CysGly) into a variety of hydrophobic and electrophilic compounds to direct them to specific sites both intra- and extracellularly. GSTs protect tissues against oxidative stress or from toxic products produced during xenobiotic metabolism [1,2,3]. Plant GSTs are involved in development [2,4]. Plant GSTs have been mainly divided into eight classes: phi, tau, lambda, theta, zeta, EF1Bg, dehydroascorbate reductase (DHAR), and tetrachlorohydroquinone dehalogenase (TCHQD) [5,6,7,8]. Phi, tau, DHAR, and lambda GSTs are specific to plants. Two new GST classes, hemerythrin and iota, were identified in Physcomitrella patens that is a nonvascular representative of early land plants [9]. Phi and tau GSTs are the most abundant in plant and are involved mainly in xenobiotic metabolism [3,10].

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