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Human TRP14 gene homologue from amphioxus Branchiostoma belcheri : identification, evolution, expression and functional characterization
Author(s) -
Jiang Shengjuan,
Zhang Shicui,
Vuthiphandchai Verapong,
Nimrat Subuntith
Publication year - 2007
Publication title -
journal of anatomy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 118
eISSN - 1469-7580
pISSN - 0021-8782
DOI - 10.1111/j.1469-7580.2007.00722.x
Subject(s) - biology , open reading frame , gene , in situ hybridization , deuterostome , conserved sequence , intron , exon , gene expression , peptide sequence , genetics , microbiology and biotechnology , phylogenetics
Thioredoxin‐related protein of 14 kDa, TRP14, has previously been identified only in humans. Here we report the identification and expression of an amphioxus TRP14 gene, named AmphiTRP14 , the first such data in a non‐mammalian organism. AmphiTRP14 consists of a 372‐bp open reading frame coding for a 123‐amino‐acid protein with a calculated molecular weight of 14 kDa. It shares 56% identity with human TRP14 and possesses a highly conserved motif CPDC. Sequence comparison suggests the evolutionary appearance of the four‐exon‐three‐intron organization of TRP14 genes after the split of protostome/deuterostome, which is highly conserved since then. AmphiTRP14 has been successfully expressed in Escherichia coli and purified. The recombinant protein exhibited features characteristic of human TRP14, including a reductase activity towards insulin. Both in situ hybridization histochemistry and immunohistochemistry revealed that AmphiTRP14 was expressed in a tissue‐specific manner, with the most abundant expression in the hepatic caecum, ovary and hind‐gut. This suggests that AmphiTRP14 plays a fundamental but tissue‐specific role, or alternatively reflects differences in the tissue susceptibility to oxidative damage.