Cytosolic glyceraldehyde-3-P dehydrogenase and the B subunit of the chloroplast enzyme are present in the pea leaf nucleus

Anderson, Louise E.; Ringenberg, M. R.; Carol, Andrew A.

doi:10.1007/s00709-003-0030-6

Cited by 27 publications

(12 citation statements)

References 34 publications

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“…Anderson et al (2004) have shown by immunogold localization the presence of GAPC both in the cytosol and the nucleus of pea leaf cells. Holtgrefe et al (2008) have proposed that, in Arabidopsis protoplasts, both GAPC1 and GAPC2 could localize also in the nucleus, in addition to the cytosol, and bind DNA.…”

Section: Discussionmentioning

confidence: 91%

Nuclear Accumulation of Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenase in Cadmium-Stressed Arabidopsis Roots

et al. 2013

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NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme involved in the glycolytic pathway. It has been widely demonstrated that mammalian GAPDH, in addition to its role in glycolysis, fulfills alternative functions mainly linked to its susceptibility to oxidative posttranslational modifications. Here, we investigated the responses of Arabidopsis (Arabidopsis thaliana) cytosolic GAPDH isoenzymes GAPC1 and GAPC2 to cadmium-induced stress in seedlings roots. GAPC1 was more responsive to cadmium than GAPC2 at the transcriptional level. In vivo, cadmium treatments induced different concomitant effects, including (1) nitric oxide accumulation, (2) cytosolic oxidation (e.g. oxidation of the redox-sensitive Green fluorescent protein2 probe), (3) activation of the GAPC1 promoter, (4) GAPC1 protein accumulation in enzymatically inactive form, and (5) strong relocalization of GAPC1 to the nucleus. All these effects were detected in the same zone of the root tip. In vitro, GAPC1 was inactivated by either nitric oxide donors or hydrogen peroxide, but no inhibition was directly provided by cadmium. Interestingly, nuclear relocalization of GAPC1 under cadmium-induced oxidative stress was stimulated, rather than inhibited, by mutating into serine the catalytic cysteine of GAPC1 (C155S), excluding an essential role of GAPC1 nitrosylation in the mechanism of nuclear relocalization, as found in mammalian cells. Although the function of GAPC1 in the nucleus is unknown, our results suggest that glycolytic GAPC1, through its high sensitivity to the cellular redox state, may play a role in oxidative stress signaling or protection in plants.

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Section: Discussionmentioning

confidence: 91%

Nuclear Accumulation of Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenase in Cadmium-Stressed Arabidopsis Roots

et al. 2013

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“…To date, a number of GAPC genes have been isolated and characterized from different species (Smith and Leong 1990;Jeong et al 2000;Anderson et al 2004). Increasing evidence indicates that GAPC displays important functional diversity in mammalian and plants (Sirover 1999(Sirover , 2005Hajirezaei et al 2006;Rius et al 2008).…”

Section: Discussionmentioning

confidence: 99%

Overexpression of a cytosolic glyceraldehyde-3-phosphate dehydrogenase gene OsGAPC3 confers salt tolerance in rice

Zhang

Rao

Shi

et al. 2011

Plant Cell Tiss Organ Cult

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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a highly conserved glycolytic enzyme that plays an important role in carbon economy. However, recent analyses of GAPDH demonstrate that GAPDH is a multifunctional protein that has roles in various cellular functions. In this study, three putative cytosolic GAPDH protein sequences (OsGAPC1-3) were identified from the rice (Oryza sativa) genome. The OsGAPC family has similar exon-intron structures. OsGAPCs transcripts were highly present in seedling shoots and roots, booting leaves, and flowers, but are at low levels in booting culms. Three OsGAPC genes are responsive to all the abiotic stresses including osmotic (20% PEG 6000), salt (200 mM NaCl), heat (42°C), abscisic acid (50 lM) and methyl viologen (50 lM) treatments. Transient expression of GFP-Os-GAPC3 fusion protein in onion epidermal cells revealed that OsGAPC3 was indeed a cytosolic protein. One of the representative OsGAPC genes, OsGAPC3, which was induced most significantly by salt stress, was overexpressed in japonica rice Zhonghua 11 under the control of a ubiquitin promoter. Transgenic rice plants overexpressing OsGAPC3 showed enhanced tolerance to salt stress. Furthermore, we found that OsGAPC3 could alleviate the salt toxicity through the regulation of hydrogen peroxide (H 2 O 2 ) levels. Taken together, these results indicate that OsGAPC3 plays important roles in salt stress tolerance in rice.

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“…Therefore, these results open the possibility that Arabidopsis GAPC1 has the ability to participate in nonglycolytic functions, as shown previously for its mammalian counterpart that participates in different regulatory and signaling functions triggered by RPTM of its catalytic cysteine and subsequent nuclear relocalization. Different plant GAPDH isoforms, including Arabidopsis GAPC1, may localize in the nucleus under certain conditions (64,(83)(84)(85). Although the function of GAPC1 in the nucleus is still unclear, nuclear relocalization is stimulated by stress conditions that also induce RPTMs of active site GAPDH cysteine (83,85).…”

Section: Discussionmentioning

confidence: 99%

Mechanisms of Nitrosylation and Denitrosylation of Cytoplasmic Glyceraldehyde-3-phosphate Dehydrogenase from Arabidopsis thaliana

Zaffagnini

Morisse

Bedhomme

et al. 2013

Journal of Biological Chemistry

106

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Background: Plant cytoplasmic GAPDH undergoes nitrosylation and glutathionylation. Results: GSNO triggers mainly nitrosylation of Arabidopsis GAPDH, which can be denitrosylated by GSH but not by thioredoxins. Conclusion: The extent of GAPDH nitrosylation is dependent on the [GSH]/[GSNO] ratio but independent of the [GSH]/ [GSSG] ratio.Significance: The mechanisms of GAPDH nitrosylation are delineated, and the prominent role of glutathione is established.

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Cytosolic glyceraldehyde-3-P dehydrogenase and the B subunit of the chloroplast enzyme are present in the pea leaf nucleus

Cited by 27 publications

References 34 publications

Nuclear Accumulation of Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenase in Cadmium-Stressed Arabidopsis Roots

Nuclear Accumulation of Cytosolic Glyceraldehyde-3-Phosphate Dehydrogenase in Cadmium-Stressed Arabidopsis Roots

Overexpression of a cytosolic glyceraldehyde-3-phosphate dehydrogenase gene OsGAPC3 confers salt tolerance in rice

Mechanisms of Nitrosylation and Denitrosylation of Cytoplasmic Glyceraldehyde-3-phosphate Dehydrogenase from Arabidopsis thaliana

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