Characterization and expression of p23 gene in the amphioxus Branchiostoma belcheri

2006 ◽  
Vol 145 (1) ◽  
pp. 10-15 ◽  
Author(s):  
Bosheng Zhao ◽  
Shicui Zhang ◽  
Yongjun Wang ◽  
Zhenhui Liu ◽  
Dexin Kong
Keyword(s):  
Branchiostoma Belcheri ◽  
P23 Gene

Unique Asymmetric Protrusion of Nerve Cord in the Amphioxus, Branchiostoma belcheri

1999 ◽  
Vol 86 (7) ◽  
pp. 328-330 ◽  
Author(s):  
Kiyoshi Terakado ◽  
Kaoru Kubokawa ◽  
Masumi Nozaki
Keyword(s):  
Nerve Cord ◽  
Branchiostoma Belcheri

Identification and functional characterization of legumain in amphioxus Branchiostoma belcheri

2009 ◽  
Vol 30 (3) ◽  
pp. 177-186 ◽  
Author(s):  
Lei Teng ◽  
Hiroshi Wada ◽  
Shicui Zhang
Keyword(s):  
Functional Characterization ◽  
Specific Substrate ◽  
Glycosylation Sites ◽  
Branchiostoma Belcheri ◽  
Hen’S Egg ◽  
Hind Gut ◽  
Catalytic Dyad ◽  
Pepstatin A

Legumain has been reported from diverse sources such as plants, parasites (animals) and mammals, but little is known in the lower chordates. The present study reports the first characterization of legumain cDNA from the protochordate Branchiostoma belcheri. The deduced 435-amino-acid-long protein is structurally characterized by the presence of a putative N-terminal signal peptide, a peptidase_C13 superfamily domain with the conserved Lys123-Gly124-Asp125 motif and catalytic dyad His153 and Cys195 and two potential Asn-glycosylation sites at Asn85 and Asn270. Phylogenetic analysis demonstrates that B. belcheri legumain forms an independent cluster together with ascidian legumain, and is positioned at the base of vertebrate legumains, suggesting that B. belcheri legumain gene may represent the archetype of vertebrate legumain genes. Both recombinant legumain expressed in yeast and endogenous legumain are able to be converted into active protein of ~37 kDa via a C-terminal autocleavage at acid pH values. The recombinant legumain efficiently degrades the legumain-specific substrate Z-Ala-Ala-Asn-MCA (benzyloxycarbonyl-L-alanyl-L-alanyl-L-asparagine-4-methylcoumaryl-7-amide) at optimum pH 5.5; and the enzymatic activity is inhibited potently by iodoacetamide and N-ethylmaleimide, partially by hen's-egg white cystatin, but not by E-64 [trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane], PMSF and pepstatin A. In addition, legumain is expressed in vivo in a tissue-specific manner, with main expression in the hepatic caecum and hind-gut of B. belcheri. Altogether, these results suggest that B. belcheri legumain plays a role in the degradation of macromolecules in food.

scholarly journals Human TRP14 gene homologue from amphioxus Branchiostoma belcheri: identification, evolution, expression and functional characterization

2007 ◽  
Vol 210 (5) ◽  
pp. 555-564 ◽  
Author(s):  
Shengjuan Jiang ◽  
Shicui Zhang ◽  
Verapong Vuthiphandchai ◽  
Subuntith Nimrat
Keyword(s):  
Functional Characterization ◽  
Branchiostoma Belcheri ◽  
Gene Homologue

Laboratory observation on spawning, fecundity and larval development of amphioxus (Branchiostoma belcheri Tsingtaunese)

1994 ◽  
Vol 12 (4) ◽  
pp. 289-294 ◽  
Author(s):  
Wu Xian-han ◽  
Zhang Shi-cui ◽  
Wang Yong-yuan ◽  
Zhang Bao-lu ◽  
Qu Yan-mei ◽  
...  
Keyword(s):  
Larval Development ◽  
Laboratory Observation ◽  
Branchiostoma Belcheri
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