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Molecular and functional characterization of a cyclophilin with antifungal activity from Chinese cabbage
- Authors
- Lee, Jung Ro; Park, Seong-Cheol; Kim, Jin-Young; Lee, Seung Sik; Park, Yoonkyung; Cheong, Gang-Won; Hahm, Kyung-Soo; Lee, Sang Yeol
- Issue Date
- 16-Feb-2007
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- antifungal activity; Chinese cabbage; cyclophilin; peptidyl-prolyl cis-trans isomerase
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.353, no.3, pp 672 - 678
- Pages
- 7
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 353
- Number
- 3
- Start Page
- 672
- End Page
- 678
- ISSN
- 0006-291X
1090-2104
- Abstract
- An antifungal protein that inhibits the growth of filamentous fungal pathogens was isolated from Chinese cabbage (Brassica campestris L. ssp. pekinensis) by affinity chromatography on Affi-gel blue gel and ion exchange chromatography on CM-Sepharose. The N-terminal amino acid sequence of the protein was highly homologous to that of plant cyclophilins and consequently the protein was denoted as C-CyP. To understand the antifungal activity of C-CyP, we isolated a cDNA encoding its gene from a Chinese cabbage leaf cDNA library. The Chinese cabbage genome bears more than one C-CyP gene copy and C-CyP mRNA is highly expressed in all tissues except the seeds. Recombinant C-CyP catalyzed the cis-trans inter-conversion of the Ala-Pro bond of the substrate, which indicates this protein has peptidyl-prolyl cis-trans isomerase activity. It also inhibited the growth of several fungal pathogens. (c) 2006 Elsevier Inc. All rights reserved.
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