Open AccessThe pro‐region of S treptomyces hygroscopicus transglutaminase affects its secretion by E scherichia coli
Author(s) -
Liu Song,
Zhang Dongxu,
Wang Miao,
Cui Wenjing,
Chen Kangkang,
Liu Yi,
Du Guocheng,
Chen Jian,
Zhou Zhemin
Publication year - 2011
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2011.02387.x
Subject(s) - streptomyces hygroscopicus , escherichia coli , tissue transglutaminase , secretion , signal peptide , biochemistry , zymogen , streptomyces , biology , recombinant dna , enzyme , secretory protein , chemistry , bacteria , genetics , gene
S treptomyces transglutaminase ( TG ase) is secreted as a zymogen (pro‐ TG ase) in liquid cultures and is then processed by the removal of its N ‐terminal region, resulting in active TG ase. To date, there is no report describing TG ase (or pro‐ TG ase) secretion in E scherichia coli . In this study, the pro‐ TG ase from S treptomyces hygroscopicus was efficiently secreted by E . coli BL 21( DE 3) using the TG ase signal peptide or the pel B signal peptide. The secreted pro‐ TG ase was efficiently transformed into active TG ase by adding dispase to the culture supernatant of the recombinant strains. Mutational analysis showed that deletion of the first six amino acids of the N ‐terminal of the pro‐region reduced the secretion of pro‐ TG ase, and removal of the next 10 amino acids resulted in the formation of insoluble pro‐ TG ase. These results suggest that the pro‐region of TG ase is essential for its efficient secretion and solubility in E . coli .