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Structure And Temperature Regulated Expression Of A Cysteine Proteinase Gene In Pachysandra Terminalis Sieb. & Zucc., Suping Zhou, Roger Sauve, Fur-Chi Chen
Structure And Temperature Regulated Expression Of A Cysteine Proteinase Gene In Pachysandra Terminalis Sieb. & Zucc., Suping Zhou, Roger Sauve, Fur-Chi Chen
Agricultural and Environmental Sciences Faculty Research
A cysteine proteinase gene (DQ403257) with an open reading frame of 1125 base pairs was isolated from Pachysdandra terminalis. The primary translated peptide has a predicted length of 374 amino acids, pI (isoelectric point) of 5.70, and molecular mass of 40.9 kDa. The Peptidase_C1 domain is between residue 141 and 367. The proteinase has a conserved motif Gly-Xaa-Thy-Xaa-Phe-Xaa-Asn in the pro region. Sequence comparison shows that the deduced peptide shares 82% identity with the cysteine proteinase RD19a precursor (RD19) (accession P43296) from Arabidopsis thaliana (L.) Heynh. Real-time quantitative reverse-transcriptase–polymerase chain reaction revealed that the gene is induced by treatments of …