scholarly journals The putative β-glucosidase BGL3I regulates cellulase induction in Trichoderma reesei

2018 ◽  
Vol 11 (1) ◽  
Author(s):  
Gen Zou ◽  
Yanping Jiang ◽  
Rui Liu ◽  
Zhihua Zhu ◽  
Zhihua Zhou
2016 ◽  
Vol 6 (2) ◽  
pp. 96-102
Author(s):  
Kouichi Nozaki ◽  
Boyang Guo ◽  
Satoshi Hatanaka ◽  
Peter Biely ◽  
Yoshihiko Amano

PLoS ONE ◽  
2013 ◽  
Vol 8 (5) ◽  
pp. e62631 ◽  
Author(s):  
Christa Ivanova ◽  
Jenny A. Bååth ◽  
Bernhard Seiboth ◽  
Christian P. Kubicek

2020 ◽  
Vol 13 (1) ◽  
Author(s):  
Sami Havukainen ◽  
Mari Valkonen ◽  
Kari Koivuranta ◽  
Christopher P. Landowski

Abstract Background Trichoderma reesei is an ascomycete fungus that has a tremendous capability of secreting extracellular proteins, mostly lignocellulose-degrading enzymes. Although many aspects of the biology of this organism have been unfolded, the roles of the many sugar transporters coded in its genome are still a mystery with a few exceptions. One of the most interesting sugar transporters that has thus far been discovered is the cellulose response transporter 1 (CRT1), which has been suggested to be either a sugar transporter or a sensor due to its seemingly important role in cellulase induction. Results Here we show that CRT1 is a high-affinity cellobiose transporter, whose function can be complemented by the expression of other known cellobiose transporters. Expression of two sequence variants of the crt1 gene in Saccharomyces cerevisiae revealed that only the variant listed in the RUT-C30 genome annotation has the capability to transport cellobiose and lactose. When expressed in the $$\Delta$$ Δ crt1 strain, the variant listed in the QM6a genome annotation offers partial complementation of the cellulase induction, while the expression of the RUT-C30 variant or cellobiose transporters from two other fungal species fully restore the cellulase induction. Conclusions These results add to our knowledge about the fungal metabolism of cellulose-derived oligosaccharides, which have the capability of inducing the cellulase production in many species. They also help us to deepen our understanding of the T. reesei lactose metabolism, which can have important consequences as this sugar is used as the inducer of protein secretion in many industrial processes which employ this species.


1980 ◽  
Vol 185 (2) ◽  
pp. 515-519 ◽  
Author(s):  
M Inglin ◽  
B A Feinberg ◽  
J R Loewenberg

A new intracellular beta-glucosidase was isolated from Trichoderma reesei. It was sequentially purified by (NH4)2SO4 precipitation and chromatography and rechromatography on Sephadex G-150. The enzyme has a mol.wt. of 98 000, optimal activity at pH 6.5, pI 4.4 and Km values of 6.7 mM and 3.3 mM for sophorose and cellobiose respectively. Possible functions of the enzyme may be regulation of cellulase induction and/or to serve as a proenzyme.


2014 ◽  
Vol 13 (8) ◽  
pp. 1001-1013 ◽  
Author(s):  
Jintao Xu ◽  
Guolei Zhao ◽  
Yanbo Kou ◽  
Weixin Zhang ◽  
Qingxin Zhou ◽  
...  

ABSTRACT Lactose (1,4- O -β- d -galacto-pyranosyl- d -glucose) induces cellulolytic enzymes in Trichoderma reesei and is in fact one of the most important soluble carbon sources used to produce cellulases on an industrial level. The mechanism underlying the induction is, however, not fully understood. In this study, we investigated the cellular functions of the intracellular β-glucosidases CEL1a and CEL1b in the induction of cellulase genes by lactose in T. reesei . We demonstrated that while CEL1a and CEL1b were functionally equivalent in mediating the induction, the simultaneous absence of these intracellular β-glucosidases abolished cbh1 gene expression on lactose. d -Galactose restored the efficient cellulase gene induction in the Δ cel1a strain independently of its reductive metabolism, but not in the Δ cel1a Δ cel1b strain. A further comparison of the transcriptional responses of the Δ cel1a Δ cel1b strain complemented with wild-type CEL1a or a catalytically inactive CEL1a version and the Δ cel1a strain constitutively expressing CEL1a or the Kluyveromyces lactis β-galactosidase LAC4 showed that both the CEL1a protein and its glycoside hydrolytic activity were indispensable for cellulase induction by lactose. We also present evidence that intracellular β-glucosidase-mediated lactose induction is further conveyed to XYR1 to ensure the efficiently induced expression of cellulase genes.


2014 ◽  
Vol 31 ◽  
pp. S216
Author(s):  
Dante Poggi-Parodi ◽  
Aurelie Pirayre ◽  
Thomas Portnoy ◽  
Hugues Mathis ◽  
Thiziri Aouam ◽  
...  

1995 ◽  
Vol 16 (4) ◽  
pp. 687-697 ◽  
Author(s):  
Robert L. Mach ◽  
Bernhard Seiboth ◽  
Andrey Myasnikov ◽  
Ramon Gonzalez ◽  
Josef Strauss ◽  
...  

2015 ◽  
Vol 8 (1) ◽  
Author(s):  
Yosuke Shida ◽  
Kaori Yamaguchi ◽  
Mikiko Nitta ◽  
Ayana Nakamura ◽  
Machiko Takahashi ◽  
...  

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