ArticlePloS one2018
Glycerol-3-phosphate dehydrogenase (GPDH) gene family in Zea mays L.: Identification, subcellular localization, and transcriptional responses to abiotic stresses.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 19 citations in OpenAlex.
- Lipid-sugar conversion regulates early white clover (Trifolium repens) seedling establishment under cadmium stress.Planta · 2025Article
- Comprehensive genomic characterization of the soybean G3PDH gene family and its role in virus resistance.BMC plant biology · 2025Article
- Enhanced Stress Tolerance in Rice Through Overexpression of a Chimeric Glycerol-3-Phosphate Dehydrogenase (OEGD).Plants (Basel, Switzerland) · 2025Article
- A Knockout of theGenes · 2025Article
- Long non-coding RNAs and their potential function in response to postharvest senescence of Sparassis latifolia during cold storage.Scientific reports · 2024Article
- Genome-Wide Identification of Cotton (Plants (Basel, Switzerland) · 2022Article
- Identification of the key functional genes in salt-stress tolerance of Cyanobacterium3 Biotech · 2021Article
- SystematicFrontiers in chemistry · 2021Article
- Embryonic developmental arrest in the annual killifish Austrolebias charrua: A proteomic approach to diapause III.PloS one · 2021Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the formation of glycerol-3-phosphate, and plays an essential role in glycerolipid metabolism and in response to various stresses in different species. In this study, six ZmGPDH genes were obtained by a thorough search against maize genome, and designated as ZmGPDH1-6, respectively. The structural and evolutionary analyses showed that the ZmGPDHs family had typical conserved domains and similar protein structures as the known GPDHs from other plant species. ZmGPDHs were divided into NAD+-dependent type A form (ZmGPDH1-5) and FAD-dependent type B form (ZmGPDH6) based on their N-terminal sequences. Four full length ZmGPDHs were fused with GFP fusion proteins, and their subcellular localization was determined. ZmGPDH1 and ZmGPDH3 were located to the cytosol and mainly recruited to the surface of endoplasmic reticulum (ER), whereas ZmGPDH4 and ZmGPDH5 were located in the chloroplast. The transcriptional analysis of the ZmGPDHs in different maize tissues revealed relatively high level of transcripts accumulation of ZmGPDHs in roots and early stage developing seeds. Furthermore, we examined the transcriptional responses of the six GPDH genes in maize under various abiotic stresses, including salt, drought, alkali and cold, and significant induction of ZmGPDHs under osmotic stresses was observed. Together, this work will provide useful information for deciphering the roles of GPDHs in plant development and abiotic stress responses.
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