Differential expression of 10 sweetpotato peroxidase genes in response to bacterial pathogen, Pectobacterium chrysanthemi

被引:37
作者
Jang, IC
Park, SY
Kim, KY
Kwon, SY
Kim, JG
Kwak, SS
机构
[1] KRIBB, Lab Environm Biotechnol, Taejon 305806, South Korea
[2] Kyungpook Natl Univ, Dept Microbiol, Taegu 702701, South Korea
关键词
Ipomoea batatas; biotic stress; convolvulaceae; native gel analysis; northern analysis; peroxidase; Pectobacterium chrysanthemi;
D O I
10.1016/j.plaphy.2004.04.002
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
To understand the function of each peroxidase (POD, EC 1.11.1.7) in terms of biotic stress, changes in POD specific activity and expression of 10 POD genes were investigated in four cultivars of sweetpotato (Ipomoea hatatas) after infection with Pectobacterium chrysanthemi. POD specific activity (units mg(-1) protein) increased from 16 h after inoculation (HAI) in three varieties. POD activities of two cultivars, Shinwhangmi and White Star, reached a maximum level at 24 HAI by about three times compared to mock treatment (NIT), and then decreased, whereas those of Zami and Yulmi continuously increased until 36 HAI. Native gel analysis revealed that one POD isoenzyme with a high electrophoretic mobility significantly increased in response to pathogen infection in all cultivars. Additionally, 10 POD genes displayed differential expression patterns upon bacterial infection by northern analysis. Several POD genes such as swpa2, swpa3, swpa4, swpa5, swpb1 were induced upon bacterial infection, but other genes were not. Particularly, swpa4 gene was markedly expressed in response to bacterial infection in four different cultivars, suggesting that this gene has a stress-inducible promoter. These results indicate that some specific POD isoenzymes are involved in defense in relation to pathogenesis of P. chrysanthemi in sweetpotato plants. (C) 2004 Elsevier SAS. All rights reserved.
引用
收藏
页码:451 / 455
页数:5
相关论文
共 32 条
[1]   A lignin-specific peroxidase in tobacco whose antisense suppression leads to vascular tissue modification [J].
Blee, KA ;
Choi, JW ;
O'Connell, AP ;
Schuch, W ;
Lewis, NG ;
Bolwell, GP .
PHYTOCHEMISTRY, 2003, 64 (01) :163-176
[2]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[3]  
CASTILLO FJ, 1992, PLANT PEROXIDASES 19, P187
[4]  
CHITTOOR JM, 1997, MOL PLANT MICROBE IN, V7, P861
[5]   A peroxidase gene promoter induced by phytopathogens and methyl jasmonate in transgenic plants [J].
Curtis, MD ;
Rae, AL ;
Rusu, AG ;
Harrison, SJ ;
Manners, JM .
MOLECULAR PLANT-MICROBE INTERACTIONS, 1997, 10 (03) :326-338
[6]  
Esnault R., 1994, PLANT PEROXIDASE NEW, V3, P7
[7]   IMMUNOCYTOCHEMICAL LOCALIZATION AND TIME COURSE OF APPEARANCE OF AN ANIONIC PEROXIDASE ASSOCIATED WITH SUBERIZATION IN WOUND-HEALING POTATO-TUBER TISSUE [J].
ESPELIE, KE ;
FRANCESCHI, VR ;
KOLATTUKUDY, PE .
PLANT PHYSIOLOGY, 1986, 81 (02) :487-492
[8]  
FRY SC, 1986, ANNU REV PLANT PHYS, V37, P165, DOI 10.1146/annurev.arplant.37.1.165
[9]   STRUCTURE OF THE HORSERADISH-PEROXIDASE ISOZYME-C GENES [J].
FUJIYAMA, K ;
TAKEMURA, H ;
SHIBAYAMA, S ;
KOBAYASHI, K ;
CHOI, JK ;
SHINMYO, A ;
TAKANO, M ;
YAMADA, Y ;
OKADA, H .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1988, 173 (03) :681-687
[10]   A large family of class III plant peroxidases [J].
Hiraga, S ;
Sasaki, K ;
Ito, H ;
Ohashi, Y ;
Matsui, H .
PLANT AND CELL PHYSIOLOGY, 2001, 42 (05) :462-468