AtPGK2, a member of PGKs gene family in Arabidopsis, has a positive role in salt stress toleranceby Dong Liu, Weichun Li, Jianfeng Cheng, Ling Hou

Plant Cell Tiss Organ Cult

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Year
2014
DOI
10.1007/s11240-014-0601-6
Subject
Horticulture

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ORIGINAL PAPER

AtPGK2, a member of PGKs gene family in Arabidopsis, has a positive role in salt stress tolerance

Dong Liu • Weichun Li • Jianfeng Cheng •

Ling Hou

Received: 17 July 2014 / Accepted: 18 August 2014 / Published online: 23 August 2014  Springer Science+Business Media Dordrecht 2014

Abstract Phosphoglycerate kinase (PGK) plays a critical role not only in photosynthetic carbon metabolism but also in glycolysis and gluconeogenesis. Although a large number of PGKs have been cloned and purified from a variety of plant sources, their physiological functions in response to abiotic stresses still remain elusive. Here we identified and characterized a member of PGKs gene family, AtPGK2, from Arabidopsis thaliana. Sequence analysis showed that AtPGK2 had high sequence similarity to PGKs proteins from other species. By using quantitative reverse transcription-polymerase chain reaction and histochemical b-glucuronidase assays, we demonstrated that AtPGK2 was mainly expressed in germinating seeds and flowers, and it could be induced significantly by salt stress. Through morphological and physiological analyses, we found that over-expression of AtPGK2 conferred salt tolerance in transgenic Arabidopsis plants. Furthermore, AtPGK2overexpressing plants showed enhanced expression of stress-responsive marker genes, including RD29A, RD29B,

KIN1 and KIN2. Collectively, our results suggested that over-expression of AtPGK2 in Arabidopsis decreased plant sensitivity to salt stress, and AtPGK2 may play a positive role in salt stress tolerance. To our knowledge, this is the first study on the physiological functions of PGK in response to salt stress in higher plants.

Keywords Arabidopsis thaliana  AtPGK2 

Salt tolerance

Abbreviations

BPG Bisphosphoglycerate

CaMV Cauliflower mosaic virus

CDS Coding sequence

Col Columbia-0

GUS b-Glucuronidase kDa Kilodaltons

MW Molecular weight

PG Phosphoglycerate

PGK Phosphoglycerate kinase pI Isoelectric poin

RT-PCR Reverse transcription-polymerase chain reaction

Introduction

Soil salinity is one of the major abiotic stresses that adversely influences on growth, development and productivity of plants. Accordingly, plants respond and adapt to salt stress through a series of morphological, physiological, and molecular changes (Ashraf 1994; Zhu 2002; Sun et al. 2013; Xu et al. 2013; Shi et al. 2014). At the molecular level, expression of a variety of genes is induced in response to high salinity in order to facilitate plants ability to survive under salt stress (Kreps et al. 2002; Xiong et al. 2002; Bartels and Sunkar 2005; Yang et al. 2013). The proteins encoded by these genes function not only in salt stress tolerance but also in downstream regulation of gene expression and signal transduction in stress response pathways (Liu et al. 2000; Xiong et al. 2002).

Electronic supplementary material The online version of this article (doi:10.1007/s11240-014-0601-6) contains supplementary material, which is available to authorized users.

D. Liu (&)  W. Li  J. Cheng  L. Hou

College of Agronomy, Jiangxi Agricultural University,

Nanchang 330045, Jiangxi, China e-mail: liudongbio@163.com 123

Plant Cell Tiss Organ Cult (2015) 120:251–262

DOI 10.1007/s11240-014-0601-6

Phosphoglycerate kinase (PGK) is an enzyme that catalyzes the reversible transfer of the high-energy phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP. Glycolytic

PGK catalyses the ADP-dependent dephosphorylation of 1,3-BPG to 3-PG (Blake and Rice 1981). A chloroplast isoform in photosynthetic eukaryotes catalyses the reverse reaction as part of the Calvin cycle. This enzyme is important because it functions not only in photosynthetic carbon metabolism but also in glycolysis and gluconeogenesis (Martin and Schnarrenberger 1997; Watson et al. 1982).

PGK is present in all living organisms and its sequence has been highly conserved throughout evolution (Longstaff et al. 1989). A large number of PGKs have been isolated from a variety of species, including human (McCarrey and

Thomas 1987), horse (Blake et al. 1972), Pig (Scopes 1969), rabbit (Krietsch and Bucher 1970), barley (McMorrow and Bradbeer 1987, 1990), wheat (Longstaff et al. 1989), spinach (Kopke-Secundo et al. 1990; Bertsch et al. 1993), pea (Pacold and Anderson 1975), Arabidopsis (Lobler 1998), tobacco (Rao et al. 1995), Chlamydomonas reinhardtii (Kitayama and Togasaki 1995) and Escherichia coli (Alefounder and Perham 1989). In humans, two isozymes of PGK have been so far identified, PGK1 and

PGK2. The isozymes have 87–88 % identical amino acid sequence identity and though structurally similar, they have different localizations: PGK2 is unique to meiotic and postmeiotic spermatogenic cells, while PGK1 is ubiquitously expressed in all cells (Michelson et al. 1985; McCarrey and Thomas 1987; Chiarelli et al. 2012). In green plants this enzyme has been shown to exist in both the chloroplasts and the cytoplasm (McMorrow and Bradbeer 1987, 1990; Kopke-Secundo et al. 1990; Shah and

Bradbeer 1994). The nuclear-encoded chloroplast PGK proteins contain N-terminal transit peptide sequences that facilitate the transfer of these proteins from the cytoplasm to the chloroplast (Rao et al. 1995). In pea shoots, cytosolic and chloroplastic PGKs have been separated by isoelectric focusing and been characterized (Pacold and Anderson 1975; Banks et al. 1979). The two forms of PGKs have been also identified from wheat and spinach (Longstaff et al. 1989; Kopke-Secundo et al. 1990; Bertsch et al. 1993). Based on the deduced amino acid sequences, these plant PGKs show significant similarity with each other and share conserved amino acid residues peculiar to prokaryotic PGKs (Kitayama and Togasaki 1995). Although a large number of PGKs have been isolated and purified from a variety of plant sources, their physiological functions in response to abiotic stresses still remain elusive.

In this study, we present data on AtPGK2, a member of