Premium
Rce1, a novel transcriptional repressor, regulates cellulase gene expression by antagonizing the transactivator Xyr1 in Trichoderma reesei
Author(s) -
Cao Yanli,
Zheng Fanglin,
Wang Lei,
Zhao Guolei,
Chen Guanjun,
Zhang Weixin,
Liu Weifeng
Publication year - 2017
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13685
Subject(s) - trichoderma reesei , repressor , cellulase , transactivation , chromatin immunoprecipitation , transcription factor , biology , regulation of gene expression , gene expression , electrophoretic mobility shift assay , promoter , gene , transcription (linguistics) , microbiology and biotechnology , transcriptional regulation , psychological repression , biochemistry , enzyme , linguistics , philosophy
Summary Cellulase gene expression in the model cellulolytic fungus Trichoderma reesei is supposed to be controlled by an intricate regulatory network involving multiple transcription factors. Here, we identified a novel transcriptional repressor of cellulase gene expression, Rce1. Disruption of the rce1 gene not only facilitated the induced expression of cellulase genes but also led to a significant delay in terminating the induction process. However, Rce1 did not participate in Cre1‐mediated catabolite repression. Electrophoretic mobility shift (EMSA) and DNase I footprinting assays in combination with chromatin immunoprecipitation (ChIP) demonstrated that Rce1 could bind directly to a cbh1 (cellobiohydrolase 1‐encoding) gene promoter region containing a cluster of Xyr1 binding sites. Furthermore, competitive binding assays revealed that Rce1 antagonized Xyr1 from binding to the cbh1 promoter. These results indicate that intricate interactions exist between a variety of transcription factors to ensure tight and energy‐efficient regulation of cellulase gene expression in T. reesei . This study also provides important clues regarding increased cellulase production in T. reesei .