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Characterization of a heat-stable protein with antimicrobial activity from Arabidopsis thaliana.

Abstract：

:A heat-stable protein with antimicrobial activity was isolated from Arabidopsis thaliana plants by buffer-soluble extraction and two chromatographic procedures. The results of MALDI-TOF analysis revealed that the isolated protein shares high sequence identity with aspen SP1. To determine the exact antimicrobial properties of this protein, a cDNA encoding the protein was isolated from an A. thaliana leaf cDNA library and named AtHS1. AtHS1 mRNA was induced by exposure to external stresses, such as salicylic acid and jasmonic acid. We also analyzed the antimicrobial activity of recombinant AtHS1 expressed in Escherichia coli. This protein inhibited pathogenic fungal strains, except for Phytophthora infestans and Phytophthora nicotianae, and it exhibited antibacterial activity against E. coli and Staphylococcus aureus. These results suggest that AtHS1 shows good potential for use as a natural material in the study of antimicrobial agents.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Park SC,Lee JR,Shin SO,Park Y,Lee SY,Hahm KS

doi

10.1016/j.bbrc.2007.07.188

subject

Has Abstract

pub_date

2007-10-26 00:00:00

pages

562-7

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)01589-6

journal_volume

362

pub_type

杂志文章

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