Cloning, characterization and antifungal activity of defensin Tfgd1 from Trigonella foenum-graecum L.
Defensins are small cysteine rich peptides with a molecular mass of 5-10 kDa and some of them exhibit potent antifungal activity. We have cloned the coding region of a cDNA of 225 bp cysteine rich defensin, named as Tfgd1, from the legume Trigonella foenum-graecum. The amino acid sequence deduced from the coding region comprised 74 amino acids, of which the N-terminal 27 amino acids constituted the signal peptide and the mature peptide comprised 47 amino acids. The protein is characterized by the presence of eight cysteine resisdues, conserved in the various plant defensins forming four disulphide bridges, which stabilize the mature peptide. The recombinant protein expressed in E coli exhibited antifungal activity against the broad host range fungus, Rhizoctonia solani and the peanut leaf spot fungus, Phaeoisariopsis personata.
Olli
Sudar
S
Department of Plant Sciences, School of Life Sciences, University of Hyderabad, India.
Kirti
P B
PB
D001203:Ascomycota / Q000187:drug effects*; D003001:Cloning, Molecular; D023082:Defensins / Q000737:chemistry / Q000235:genetics* / Q000494:pharmacology*; D008826:Microbial Sensitivity Tests; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D011993:Recombinant Fusion Proteins / Q000494:pharmacology; D012232:Rhizoctonia / Q000187:drug effects*; D017422:Sequence Analysis, DNA; D029910:Trigonella / Q000737:chemistry / Q000235:genetics / Q000502:physiology
D023082:Defensins; D010940:Plant Proteins; D011993:Recombinant Fusion Proteins