A novel defensin from the lentil Lens culinaris seeds.
A novel 47-residue plant defensin was purified from germinated seeds of the lentil Lens culinaris by ammonium sulfate precipitation, gel filtration, chromatography, and RP-HPLC. The molecular mass (5440.41Da) and complete amino acid sequence (KTCENLSDSFKGPCIPDGNCNKHCKEKEHLLSGRCRDDFRCWCTRNC) of defensin, termed Lc-def, were determined. Lc-def has eight cysteines forming four disulfide bonds. The total RNA was isolated from lentil germinated seeds, RT-PCR and subsequent cloning were performed, and cDNA was sequenced. A 74-residue predefensin contains a putative signal peptide (27 amino acid) and a mature protein. Lc-def shows high sequence homology with legumes defensins, exhibits an activity against Aspergillus niger, but does not inhibit proteolytic enzymes.
Finkina
Ekaterina I
EI
Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str. 16/10, 117997 Moscow, Russia.
Shramova
Elena I
EI
Tagaev
Andrey A
AA
Ovchinnikova
Tatiana V
TV
D000595:Amino Acid Sequence; D001234:Aspergillus niger / Q000187:drug effects*; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D023082:Defensins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D027806:Lens Plant / Q000235:genetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D010447:Peptide Hydrolases / Q000187:drug effects; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D021382:Protein Sorting Signals; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012639:Seeds / Q000235:genetics; D017422:Sequence Analysis, DNA; D014357:Trypsin / Q000737:chemistry
D018076:DNA, Complementary; D023082:Defensins; D010446:Peptide Fragments; D010940:Plant Proteins; D021382:Protein Sorting Signals; D010447:Peptide Hydrolases; D014357:Trypsin