title: Isolation of trehalose-6-phosphate phosphatase gene from tobacco and its functional analysis in yeast cells.
abstract: Trehalose is a nonreducing disaccharide composed of two glucose units joined by an alpha, alpha-1, 1 linkage, and has been found in bacteria, yeast, fungi, invertebrates and plants. Accumulation of trehalose in organisms plays a role in enhancing the stress tolerance. A trehalose-6-phosphate phosphatase gene, NtTPPL, was isolated from tobacco in this report. The predicted NtTPPL protein has a putative trehalose_PPase domain. The transcription of the NtTPPL gene was significantly induced by heat stress, and was only slightly induced by NaCl, PEG and low-temperature treatments. When expressing in yeast tps2 mutant, NtTPPL rescued the mutant phenotype under high temperature. This result indicated that NtTPPL functioned as a trehalose-6-phosphate phosphatase in yeast and may play similar roles in plants.
authors.affiliation: National Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, The Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Yu-Jun
authors.initials: YJ
authors.lastname: Wang
authors.forename: Yu-Jun
authors.initials: YJ
authors.lastname: Hao
authors.forename: Zhi-Gang
authors.initials: ZG
authors.lastname: Zhang
authors.forename: Tao
authors.initials: T
authors.lastname: Chen
authors.forename: Jin-Song
authors.initials: JS
authors.lastname: Zhang
authors.forename: Shou-Yi
authors.initials: SY
authors.lastname: Chen
mesh_terms: D000595:Amino Acid Sequence; D015870:Gene Expression; D005816:Genetic Complementation Test; D008969:Molecular Sequence Data; D009154:Mutation; D030781:Organisms, Genetically Modified; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014026:Nicotiana / Q000201:enzymology* / Q000235:genetics*
chemical_list: C023178:trehalose-phosphatase; D010744:Phosphoric Monoester Hydrolases