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| Cloning and Sequence Analysis of the CkC3H Gene from Caragana korshinskii Kom. and Preliminary Studies of Its Function |
| LI Gao1,2, YANG Qi1, ZHANG Ye1,3, WANG Rui-gang1, LI Guo-jing1 |
1. College of Life Sciences, Inner Mongolia Agricultural University, Hohhot 010018, China;
2. Beijing Summer Palace Management Office, Beijing 100091, China;
3. The Ordos Food and Drug Inspection and Research Center, Ordos 017000, China |
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Abstract Coumarate 3-Hydroxylase (C3H) is a key enzyme in lignin biosynthesis pathway. A C3H encoding gene was cloned by rapid amplification of cDNA end technique from Caragana korshinskii Kom. The full length gDNA of CkC3H was 4235bp, contained three exons and two introns. The full length of ORF was 1530bp, and the protein deduced from this cDNA comprised 509 amino acids with a calculated molecular weight of 57.61kDa and an isoelectric point of 7.67. The deduced protein contains a P450 domain and was named as CkC3H (GenBank accession no. KC309408). Phylogenetic analysis indicated that CkC3H shared the closest homology with the C3H from Glycine max. Binary vector carried the cDNA sequence of CkC3H driven by 35S promoter was constructed and transformed into the ref8 mutant of Arabidopsis thaliana. The dwarf and sterile phenotype of the ref8 mutant were partially restored by the transgene. These showed that CkC3H might have at least partially similar function with AtC3H.
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Received: 22 January 2013
Published: 25 April 2013
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