title: Molecular cloning of a potential Verticillium dahliae resistance gene SlVe1 with multi-site polyadenylation from Solanum licopersicoides.
abstract: Caused by Verticillium spp. pathogens, verticillium wilt is a common detrimental disease damaging yield production of many important crops. Isolation of verticillium wilt resistance genes and their transgenic application is a fundamental way to control this disease. Here we report the cloning and sequence characterization of a potential Verticillium dahliae Kleb. resistance gene (Ve) from Solanum lycopersicoides Dun. (designated as SlVe1). The nucleotide sequence of SlVe1 is 3400 bp with an ORF of 3156 bp encoding a protein precursor of 1051 amino acids (aa). Unlike tomato Ve1, SlVe1 had a short leader sequence of 22 bp. Multiple polyadenylation sites were detected, which may result from alternative cleavages directed by the common polyadenylation signal AATAAA, and nucleotide sequences of the cleavage sites for polyadenylation conform to PyPyA. Sharing high homologies to tomato verticillium wilt disease resistance genes Ve1 and Ve2, SlVe1 encoded a cell-surface glycoprotein with receptor-mediated endocytosis-like signal. The leucine rich (16.51%) putative SlVe1 protein had a calculated molecular weight of 116.97 kDa with an isoelectric point of 5.22. It possessed a hydrophobic N-terminal signal peptide of 23 aa and 28 predicted significant leucine-rich repeats (LRRs) containing 29 potential N-glycosylation sites (18 being significant). A membrane-associated hydrophobic domain resided within the C-terminal, flanked by a neutral/acidic aa rich domain and a neutral/basic aa rich domain. Forty-four predicted phosphorylation sites (28 for S, 5 for T and 11 for Y) distributed in SlVe1, and an endocytosis signal EKWLLW resided in the neutral/basic aa rich C-terminal domain. As compared with Ve1, several clues of variations have been detected in SlVe1 and their possible implications are discussed.
authors.affiliation: State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan-SfTU-Nottingham Plant Biotechnology R&D Center, Morgan-Tan International Center for Life Sciences, Fudan University, Shanghai 200433, People's Republic of China.
authors.forename: Yourong
authors.initials: Y
authors.lastname: Chai
authors.forename: Lingxia
authors.initials: L
authors.lastname: Zhao
authors.forename: Zhihua
authors.initials: Z
authors.lastname: Liao
authors.forename: Xiaofen
authors.initials: X
authors.lastname: Sun
authors.forename: Kaijing
authors.initials: K
authors.lastname: Zuo
authors.forename: Lei
authors.initials: L
authors.lastname: Zhang
authors.forename: Sangen
authors.initials: S
authors.lastname: Wang
authors.forename: Kexuan
authors.initials: K
authors.lastname: Tang
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D007113:Immunity, Innate / Q000235:genetics; D018551:Solanum lycopersicum / Q000235:genetics; D008562:Membrane Glycoproteins / Q000235:genetics*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000235:genetics*; D026723:Polyadenylation; D011956:Receptors, Cell Surface / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D032322:Solanum / Q000235:genetics* / Q000382:microbiology*; D020172:Verticillium / Q000235:genetics / Q000472:pathogenicity*
chemical_list: D008562:Membrane Glycoproteins; D010940:Plant Proteins; D011956:Receptors, Cell Surface; C430462:Ve1 protein, Lycopersicon esculentum