Identification, genomic organization and expression pattern of glutathione S-transferase in the silkworm, Bombyx mori

被引:129
作者
Yu, Quanyou [1 ,3 ]
Lu, Cheng [1 ]
Li, Bin [1 ]
Fang, Shoumin [2 ]
Zuo, Weidong [1 ]
Dai, Fangyin [1 ]
Zhang, Ze [1 ,3 ]
Xiang, Zhonghuai [1 ]
机构
[1] Southwest Univ, Coll Biotechnol, Key Sericultural Lab Agr Minist, Chongqing 400715, Peoples R China
[2] China W Normal Univ, Coll Life Sci, Nanchong 637002, Peoples R China
[3] Chongqing Univ, Inst Agr & Life Sci, Chongqing 400030, Peoples R China
关键词
Glutathione S-transferases; Bombyx mori; Genomic organization; Expression pattern;
D O I
10.1016/j.ibmb.2008.08.002
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
Glutathione S-transferases (GSTs) are a multifunctional supergene family and some play an important role in insecticide resistance. We have identified 23 putative cytosolic GSTs by searching the new assembly of the Bombyx mori genome sequence. Phylogenetic analyses on the amino acid sequences reveal that 21 of the B. mori GSTs fall into six classes represented in other insects, the other two being unclassified. The majority of the silkworm GSTs belong to the Delta, Epsilon, and Omega classes. Most members of each class are tandemly arranged in the genome, except for the Epsilon GSTs. Expressed sequence tags (ESTs) corresponding to 19 of the 23 GSTs were found in available databases. Furthermore RT-PCR experiments detected expression of all the GSTs in multiple tissues on day 3 of fifth instar larvae. Surprisingly, we found little or no expression of most Delta and Epsilon GSTs in the fat body, which is thought to be the main detoxification organ. This may explain the sensitivity of the silkworm to certain insecticides. Our data provide some insights into the evolution of the B. mori GST family and the functions of individual GST enzymes. (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1158 / 1164
页数:7
相关论文
共 47 条
[1]  
AKAOKA K, 2003, J INSECT BIOTECH SER, V72, P117
[2]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[3]  
[Anonymous], 1980, Reviews in Biochemical Toxicology
[4]  
[Anonymous], 1989, Cladistics, DOI DOI 10.1111/J.1096-0031.1989.TB00562.X
[5]  
Board PG, 1997, BIOCHEM J, V328, P929
[6]   Identification, characterization, and crystal structure of the omega class glutathione transferases [J].
Board, PG ;
Coggan, M ;
Chelvanayagam, G ;
Easteal, S ;
Jermiin, LS ;
Schulte, GK ;
Danley, DE ;
Hoth, LR ;
Griffor, MC ;
Kamath, AV ;
Rosner, MH ;
Chrunyk, BA ;
Perregaux, DE ;
Gabel, CA ;
Geoghegan, KF ;
Pandit, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (32) :24798-24806
[7]  
Chelvanayagam G, 2001, CHEM-BIOL INTERACT, V133, P256
[8]   GLUTATHIONE TRANSFERASE ISOZYMES OF DIAMONDBACK MOTH LARVAE AND THEIR ROLE IN THE DEGRADATION OF SOME ORGANOPHOSPHORUS INSECTICIDES [J].
CHIANG, FM ;
SUN, CN .
PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY, 1993, 45 (01) :7-14
[9]   EVIDENCE THAT DDT-DEHYDROCHLORINASE FROM THE HOUSEFLY IS A GLUTATHIONE S-TRANSFERASE [J].
CLARK, AG ;
SHAMAAN, NA .
PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY, 1984, 22 (03) :249-261
[10]   A deficit of detoxification enzymes: pesticide sensitivity and environmental response in the honeybee [J].
Claudianos, C. ;
Ranson, H. ;
Johnson, R. M. ;
Biswas, S. ;
Schuler, M. A. ;
Berenbaum, M. R. ;
Feyereisen, R. ;
Oakeshott, J. G. .
INSECT MOLECULAR BIOLOGY, 2006, 15 (05) :615-636