• BMB Reports
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• v.34 no.4
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• pp.334-341
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• 2001

Even though three isotypes of thioredoxins (-f, -m and -h types) have been identified in a variety of plant cells, there are only a few reports on thioredoxin-h that were recently identified. In this study, a cDNA encoding a h-type of thioredoxin was isolated from a cDNA library of Chinese cabbage, and named here CTrx-h. An open reading frame of the gene contained a polypeptide of 133 amino acids with a conserved active center, WCGPC, which appeared in all of the thioredoxin proteins. A deduced amino acid sequence of the CTrx-h showed the highest sequence identity with those of Arabidopsis thioredoxin-h2 (75.2%) and thioredoxin-h5 (46.6%) proteins, but it shared a low sequence homology to other isotypes of plant thioredoxinm and thioredoxin-f. The CTrx-h protein that is expressed in E. coli represented not only an insulin reduction activity, but also electron transferring activity from NADPH to thioredoxin-dependent peroxidase. A genomic Southern blot analysis using the cDNA insert of CTrx-h revealed that the gene consisted of a small multigene family in Chinese cabbage genome. On the contrary to other thioredoxin-h proteins that were widely distributed in most tissues of the plant, the CTrx-h was predominantly expressed in flowers. The expression was very low in other tissues. The data of the Northern blot analysis suggests that the CTrx-h may have other functions in flower development or differentiation, in addition to its defensive role.