Document Type
Article
Publication Date
1-2007
Abstract
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 1 to 7 days of darkness, 2 hours and 3 to 7 days at 5 °C, and 3 days at 38 °C.
Recommended Citation
Zhou, S., Sauve, R., & Chen, F. (2007). Structure and Temperature Regulated Expression of a Cysteine Proteinase Gene in Pachysandra terminalis Sieb. & Zucc., Journal of the American Society for Horticultural Science J. Amer. Soc. Hort. Sci., 132(1), 97-101. Retrieved Jun 16, 2021, from https://journals.ashs.org/jashs/view/journals/jashs/132/1/article-p97.xml