Identification and Analysis of Secretory Proteins in Bacillus thuringiensis

doi:10.13560/j.cnki.biotech.bull.1985.2017.04.022

Abstract

Abstract: The study on Bacillus thuringiensis（Bt）secretory protein types and their contents,especially the extracellular proteases,is of great significance for fully understanding the insecticidal mechanism and expanding the application of this bacterium. In our research,the secretory protein samples in the transition phase of Bt_HD73 were detected by mass spectrometry,then the types,contents,functions and signal peptides of secretory proteins were analyzed. The results showed that Bt_HD73 secreted 54 kinds of extracellular proteins in transition phase,and most of them were enzymes,accounting for 66.30% of all secretory proteins. Moreover,most of the enzymes were proteases,and the followed was virulence protein,accounting for 14.53% of all secretory proteins. Among the 54 secretory proteins,27 proteins were found to contain the classic Sec-type signal peptides,and the lengths were between 24 and 40 amino acid residues. Therefore,Bt_HD73 has a strong secretory ability,and it can secrete large amounts of enzymes especially proteases in the transition phase. Concurrently,the signal peptide library of this strain was established in this study,including 27 signal peptides with potential for guiding the secretion of heterologous proteins.

Key words: Bacillus thuringiensis, secretory expression, extracellular protease, secretory protein, signal peptide

WANG Zhi-wen, CHEN Hai-bo, SONG Fu-ping, GUO Shu-yuan. Identification and Analysis of Secretory Proteins in Bacillus thuringiensis[J]. Biotechnology Bulletin, 2017, 33(4): 169-176.

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