title: MET3 promoter: a tightly regulated promoter and its application in construction of conditional lethal strain.
abstract: The beta-galactosidase activity driven by MET3 promoter was assayed in the absence of methionine and in the presence of different concentration of methionine in medium. To compare its activity with GAL1 promoter and the data reported by Mumburg about MET25 promoter, the MET3 promoter was a weak but tightly controlled promoter. Its successful application in the construction of methionine-sensitive tri-mutant ( cln1 Delta cln2 Delta pho85 Delta) demonstrated that the MET3 promoter is a useful promoter in construction of conditional lethal strain and heterologous expression in Saccharomyces cerevisiae.
authors.affiliation: Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, The Chinese Academy of Sciences, Shanghai 200031, China.
authors.forename: Xicheng
authors.initials: X
authors.lastname: Mao
authors.forename: Yafang
authors.initials: Y
authors.lastname: Hu
authors.forename: Chao
authors.initials: C
authors.lastname: Liang
authors.forename: Changde
authors.initials: C
authors.lastname: Lu
mesh_terms: D003001:Cloning, Molecular / Q000379:methods; D018844:Cyclin-Dependent Kinases / Q000235:genetics; D016213:Cyclins / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D017930:Genes, Reporter; D008715:Methionine / Q000378:metabolism; D008958:Models, Molecular; D011401:Promoter Regions, Genetic; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics; D013430:Sulfate Adenylyltransferase / Q000235:genetics*; D001616:beta-Galactosidase / Q000096:biosynthesis / Q000235:genetics
chemical_list: C082719:CLN1 protein, S cerevisiae; C082721:CLN2 protein, S cerevisiae; D016213:Cyclins; D029701:Saccharomyces cerevisiae Proteins; D008715:Methionine; D018844:Cyclin-Dependent Kinases; C058605:PHO85 protein, S cerevisiae; D013430:Sulfate Adenylyltransferase; D001616:beta-Galactosidase