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Haijuan Fan,Zhihua Liu,Rongshu Zhang,Na Wang,Kai Dou,Gulijimila Mijiti,Guiping Diao,Zhiying Wang 한국미생물학회 2014 The journal of microbiology Vol.52 No.2
The subtilisin-like serine protease gene ThSS45 has beencloned from Trichoderma harzianum ACCC30371. Its codingregion is 1302 bp in length, encoding 433 amino acids,with a predicted protein molecular weight of 44.9 kDa andpI of 5.91. ThSS45 was shown by RT-qPCR analysis to bedifferentially transcribed in response to eight different treatments. The transcription of ThSS45 was up-regulated whengrown in mineral medium, under carbon starvation, andnitrogen starvation, and in the presence of 1% root powder,1% stem powder, and 1% leaf powder derived from Populusdavidiana × P. bolleana (Shanxin poplar) aseptic seedlings. The highest increase in transcription approached 3.5-foldthat of the control at 6 h under induction with 1% poplarroot powder. The transcription of ThSS45 was also slightlyup-regulated by 1% Alternaria alternata cell wall and 5% A. alternata fermentation liquid. Moreover, the analyses of codingand promoter regions of ThSS45 homologs indicatedthat serine protease may be involved in both mycoparasitismand antibiotic secretion. ThSS45 was cloned into the pGEX-4T-2 vector and then expressed in Escherichia coli BL21. Therecombinant protein, with an expected molecular weight ofapproximately 69 kDa, was then purified. When transformantBL21-ss was induced with 1 mM IPTG for 6 h, thepurified protease activity reached a peak of 18.25 U/ml atpH 7.0 and 40°C. In antifungal assays the purified proteaseobviously inhibited the growth of A. alternata mycelia.
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