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Molecular and functional characterization of a cyclophilin with antifungal activity from Chinese cabbage.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Lee JR,Park SC,Kim JY,Lee SS,Park Y,Cheong GW,Hahm KS,Lee SY

doi

10.1016/j.bbrc.2006.12.102

subject

Has Abstract

pub_date

2007-02-16 00:00:00

pages

672-8

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)02735-5

journal_volume

353

pub_type

杂志文章

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