PUBLICATION
Identification and expression of a novel class of glutathione-S-transferase from amphioxus Branchiostoma belcheri with implications to the origin of vertebrate liver
- Authors
- Fan, C., Zhang, S., Liu, Z., Li, L., Luan, J., and Saren, G.
- ID
- ZDB-PUB-061108-18
- Date
- 2007
- Source
- The international journal of biochemistry & cell biology 32(2): 450-461 (Journal)
- Registered Authors
- Li, Lei, Liu, Zhenhui
- Keywords
- Glutathione-S-transferases, Amphioxus, In situ hybridization, Immunohistochemistry, Hepatic caecum
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Antibody Specificity
- Chordata, Nonvertebrate/anatomy & histology
- Chordata, Nonvertebrate/enzymology*
- Chordata, Nonvertebrate/genetics*
- DNA, Complementary
- Gene Expression*
- Glutathione Transferase/chemistry
- Glutathione Transferase/genetics*
- Glutathione Transferase/immunology
- Liver/metabolism
- Molecular Sequence Data
- Organ Specificity
- Phylogeny
- Recombinant Proteins/chemistry
- Recombinant Proteins/genetics
- Recombinant Proteins/immunology
- Sequence Alignment
- Vertebrates/anatomy & histology
- Vertebrates/metabolism
- PubMed
- 17084657 Full text @ Int. J. Biochem. Cell Biol.
Citation
Fan, C., Zhang, S., Liu, Z., Li, L., Luan, J., and Saren, G. (2007) Identification and expression of a novel class of glutathione-S-transferase from amphioxus Branchiostoma belcheri with implications to the origin of vertebrate liver. The international journal of biochemistry & cell biology. 32(2):450-461.
Abstract
Glutathione-S-transferases have been identified in all the living species examined so far, yet little is known to date about them in amphioxus, a model organism for insights into the origin and evolution of vertebrates. We have isolated a cDNA encoding an amphioxus (Branchiostoma belcheri) glutathione-S-transferase with a predicted molecular mass of approximately 26kDa, from the gut cDNA library. The glutathione-S-transferase had 43.7-51.8% identity to most glutathione-S-transferases identified from aquatic organisms including fish and green alga, but it was much less identical (<27%) to other cytosolic glutathione-S-transferase classes. The phylogenetic analysis revealed that the glutathione-S-transferase was grouped together with most piscine and algal glutathione-S-transferases, separating from other cytosolic glutathione-S-transferase classes. Moreover, the glutathione-S-transferase had an exon-intron organization typical of zebrafish putative GST, red sea bream GSTR1 and plaice GSTA1 genes. The recombinant glutathione-S-transferase has been successfully expressed and purified, which showed a relatively high catalytic activity (3.37+/-0.1unit/mg) toward 1-chloro-2, 4-dinitrobenzene and a moderate activity toward ethacrynic acid (0.41+/-0.01unit/mg), although it had no detectable activity toward 1, 2-dichloro-4-nitrobenzene, 4-hydroxynonenal, 4-nitrobenzyl chloride and cumene hydroperoxide. In addition, we have revealed a tissue-specific expression pattern of the glutathione-S-transferase gene in B. belcheri, with the most abundant expression in the hepatic caecum. All these indicate that the amphioxus glutathione-S-transferase belongs to a novel rho-class of glutathione-S-transferases with a tissue-specific expression pattern. The relation between the glutathione-S-transferase expression in amphioxus hepatic caecum and the origin of vertebrate liver is also discussed.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping