The cDNA of alcohol dehydrogenase (PgADH) was isolated and characterized from the leaf of Panax ginseng. The cDNA had an open reading frame of 801 bp and a deduced amino acid sequence of 266 residues. The calculated molecular mass of the mature protein is approximately 29 kDa with a predicated isoelectric point of 6.84. Homology analysis revealed that the deduced amino acid of PgADH shares a high degree of homology with the short-chain ADH proteins of other plants. Genomic DNA hybridization analysis indicated that PgADH represents a multi-gene family. The expression of PgADH under various environmental stresses was analyzed at different time points using real-time PCR. ABA, SA and especially JA (80-fold) significantly induced PgADH expression within 24 h of treatment. The positive responses of PgADH to abiotic stimuli suggest that ginseng ADH may protect against hormone-related environmental stresses.
Isolation and characterization of a novel short-chain alcohol dehydrogenase gene from Panax ginseng.
Yu-Jin Kim,J. Shim,Jung-Hye Lee,Dae-young Jung,Hwa-Young Sun,J. In,Deok-Chun Yang
Published 2009 in BMB Reports
ABSTRACT
PUBLICATION RECORD
- Publication year
2009
- Venue
BMB Reports
- Publication date
2009-10-31
- Fields of study
Biology, Medicine, Chemistry
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
CITATION MAP
EXTRACTION MAP
CLAIMS
- No claims are published for this paper.
CONCEPTS
- No concepts are published for this paper.
REFERENCES
Showing 1-25 of 25 references · Page 1 of 1
CITED BY
Showing 1-18 of 18 citing papers · Page 1 of 1