title: Analysis of celery (Apium graveolens) mannitol dehydrogenase (Mtd) promoter regulation in Arabidopsis suggests roles for MTD in key environmental and metabolic responses.
abstract: Of the growing list of promising genes for plant improvement, some of the most versatile appear to be those involved in sugar alcohol metabolism. Mannitol, one of the best characterized sugar alcohols, is a significant photosynthetic product in many higher plants. The roles of mannitol as both a metabolite and an osmoprotectant in celery (Apium graveolens) are well documented. However, there is growing evidence that 'metabolites' can also have key roles in other environmental and developmental responses in plants. For instance, in addition to its other properties, mannitol is an antioxidant and may have significant roles in plant-pathogen interactions. The mannitol catabolic enzyme mannitol dehydrogenase (MTD) is a prime modulator of mannitol accumulation in plants. Because the complex regulation of MTD is central to the balanced integration of mannitol metabolism in celery, its study is crucial in clarifying the physiological role(s) of mannitol metabolism in environmental and metabolic responses. In this study we used transformed Arabidopsis to analyze the multiple environmental and metabolic responses of the Mtd promoter. Our data show that all previously described changes in Mtd RNA accumulation in celery cells mirrored changes in Mtd transcription in Arabidopsis. These include up-regulation by salicylic acid, hexokinase-mediated sugar down-regulation, and down-regulation by salt, osmotic stress and ABA. In contrast, the massive up-regulation of Mtd expression in the vascular tissues of salt-stressed Arabidopsis roots suggests a possible role for MTD in mannitol translocation and unloading and its interrelation with sugar metabolism.
authors.affiliation: Department of Horticultural Science, North Carolina State University, Raleigh 27695-7609, USA.
authors.forename: E
authors.initials: E
authors.lastname: Zamski
authors.forename: W W
authors.initials: WW
authors.lastname: Guo
authors.forename: Y T
authors.initials: YT
authors.lastname: Yamamoto
authors.forename: D M
authors.initials: DM
authors.lastname: Pharr
authors.forename: J D
authors.initials: JD
authors.lastname: Williamson
mesh_terms: D019325:3-O-Methylglucose / Q000494:pharmacology; D000040:Abscisic Acid / Q000494:pharmacology; D000085:Acetates / Q000494:pharmacology; D000077102:Apium / Q000201:enzymology* / Q000235:genetics; D017360:Arabidopsis / Q000166:cytology / Q000235:genetics* / Q000378:metabolism; D002455:Cell Division / Q000187:drug effects; D003517:Cyclopentanes / Q000494:pharmacology; D003847:Deoxyglucose / Q000494:pharmacology; D004305:Dose-Response Relationship, Drug; D005786:Gene Expression Regulation / Q000187:drug effects; D005947:Glucose / Q000494:pharmacology; D049452:Green Fluorescent Proteins; D008164:Luminescent Proteins / Q000235:genetics / Q000378:metabolism; D008353:Mannitol / Q000494:pharmacology; D008354:Mannitol Dehydrogenases / Q000235:genetics*; D054883:Oxylipins; D010944:Plants / Q000187:drug effects / Q000201:enzymology / Q000235:genetics; D030821:Plants, Genetically Modified / Q000166:cytology / Q000235:genetics / Q000378:metabolism; D011401:Promoter Regions, Genetic / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D020156:Salicylic Acid / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology
chemical_list: D000085:Acetates; D003517:Cyclopentanes; D008164:Luminescent Proteins; D054883:Oxylipins; D011993:Recombinant Fusion Proteins; D019325:3-O-Methylglucose; D049452:Green Fluorescent Proteins; D008353:Mannitol; D012965:Sodium Chloride; D000040:Abscisic Acid; C072239:methyl jasmonate; D003847:Deoxyglucose; D008354:Mannitol Dehydrogenases; D005947:Glucose; D020156:Salicylic Acid