Isolation and Characterization of a Formate Dehydrogenaase cDNA in Poplar(Populus alba x P. glandulosa)
2013
Bae, E.K., Korea Forest Research Institute, Suwon, Republic of Korea | Lee, H.S., Korea Forest Research Institute, Suwon, Republic of Korea | Lee, J.S., Korea Forest Research Institute, Suwon, Republic of Korea | Chou, Y.I., Korea Forest Research Institute, Suwon, Republic of Korea | Yoon, S.K., Korea Forest Research Institute, Suwon, Republic of Korea | Eo, S.H., Kongju National University, Yesan, Republic of Korea
Formate dehydrogenase (FDH), catalyzing the oxidation of the formate ion to carbon dioxide, is known as the stress protein in response to drought, low temperature and pathogen infection. To study the functions of FDH in poplar (Populus alba × P. glandulosa), we isolated a FDH cDNA (PagFDH1) and examined its expressional characteristics. The PagFDH1 is 1,499 base pairs long and encodes a putative 388 amino acid protein with an expected molecular mass of 42.5 kDa. The PagFDH1 protein has N-terminal mitochondria signal peptide and NAD+ binding domain. Southern blot analysis indicated that a single copy of the PagFDH1 is present in the poplar genome. PagFDH1 is expressed highly in the suspension cells (especially in the lag and early exponential phases) and moderately in roots, flowers and leaves. ABA-mediated enhanced expression of PagFDH1 in response to drought and salt stress treatments indicates that the gene product could play an important role in the development of stress resistant trees.
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