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

被引：39
作者：
Park, Seong-Cheol
Lee, Jung Ro
Shin, Sun-Oh
Park, Yoonkyung
Lee, Sang Yeol [1 ]
Hahin, Kyung-Soo
机构：
[1] Chosun Univ, Res Ctr Proteineous Mat, Kwangju 501759, South Korea
[2] Chosun Univ, Dept Med, Kwangju 501759, South Korea
[3] Chosun Univ, Biotechnol & BK21 Res Team Protein Activ Control, Kwangju 501759, South Korea
[4] Gyeongsang Natl Univ, Environm Biotechnol natl Core Res Ctr, Jinju 660701, South Korea
[5] Gyeongsang Natl Univ, Div Appl Life Sci, Jinju 660701, South Korea
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 362卷 / 03期
关键词：
antimicrobial activity; Arabidopsis thaliana; AtHS1; heat-stable protein;
D O I：
10.1016/j.bbrc.2007.07.188
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 SPI. 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. (c) 2007 Elsevier Inc. All rights reserved.
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收藏
页码：562 / 567
页数：6
相关论文
共 22 条
[1]   Interactions of histatin 5 and histatin 5-derived peptides with liposome membranes: surface effects, translocation and permeabilization [J].
den Hertog, AL ;
Sang, HWWF ;
Kraayenhof, R ;
Bolscher, JGM ;
Van't Hof, W ;
Veerman, ECI ;
Amerongen, AVN .
BIOCHEMICAL JOURNAL, 2004, 379 :665-672
[2]   Arabidopsis SNI1 and RAD51D regulate both gene transcription and DNA recombination during the defense response [J].
Durrant, Wendy E. ;
Wang, Shui ;
Dong, Xinnian .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (10) :4223-4227
[3]   Antimicrobial activity studies on a trypsin-chymotrypsin protease inhibitor obtained from potato [J].
Kim, JY ;
Park, SC ;
Kim, MH ;
Lim, HT ;
Park, Y ;
Hahm, KS .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2005, 330 (03) :921-927
[4]   Purification and characterization of a heat-stable serine protease inhibitor from the tubers of new potato variety "Golden Valley" [J].
Kim, Mi-Hyun ;
Park, Seong-Cheol ;
Kim, Jin-Young ;
Lee, Sun Young ;
Lim, Hak-Tae ;
Cheong, Hyeonsook ;
Hahm, Kyung-Soo ;
Park, Yoonkyung .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2006, 346 (03) :681-686
[5]  
LAEMMLI UK, 1973, J MOL BIOL, V80, P573
[6]  
Lee JR, 2007, MOL CELLS, V23, P161
[7]   Molecular and functional characterization of a cyclophilin with antifungal activity from Chinese cabbage [J].
Lee, Jung Ro ;
Park, Seong-Cheol ;
Kim, Jin-Young ;
Lee, Seung Sik ;
Park, Yoonkyung ;
Cheong, Gang-Won ;
Hahm, Kyung-Soo ;
Lee, Sang Yeol .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2007, 353 (03) :672-678
[8]   Demonstration of ribonuclease activity in the plant ribosome-inactivating proteins alpha- and beta-momorcharins [J].
Mock, JWY ;
Ng, TB ;
Wong, RNS ;
Yao, QZ ;
Yeung, HW ;
Fong, WP .
LIFE SCIENCES, 1996, 59 (22) :1853-1859
[9]   Antifungal proteins and peptides of leguminous and non-leguminous origins [J].
Ng, TB .
PEPTIDES, 2004, 25 (07) :1215-1222
[10]   New lytic peptides based on the D,L-amphipathic helix motif preferentially kill tumor cells compared to normal cells [J].
Papo, N ;
Shai, Y .
BIOCHEMISTRY, 2003, 42 (31) :9346-9354
123