Evidence map›Paper›PMID 24879125›Full record

ArticleEukaryotic cell2014

Intracellular β-glucosidases CEL1a and CEL1b are essential for cellulase induction on lactose in Trichoderma reesei.

Jintao Xu, Guolei Zhao, Yanbo Kou, Weixin Zhang, Qingxin Zhou, Guanjun Chen, Weifeng Liu

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.9field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 53 citations in OpenAlex.

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  19. Functional Studies of β-Glucosidases ofFrontiers in microbiology · 2017
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Jintao XuState Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, Shandong, People's Republic of China.
Guolei ZhaoState Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, Shandong, People's Republic of China.
Yanbo KouState Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, Shandong, People's Republic of China.
Weixin ZhangState Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, Shandong, People's Republic of China.
Qingxin ZhouInstitute of Agro-Food Science Technology, Shandong Academy of Agricultural Sciences, Jinan, People's Republic of China.
Guanjun ChenState Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, Shandong, People's Republic of China.
Weifeng LiuState Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, Shandong, People's Republic of China weifliu@sdu.edu.cn.
Shandong University · CNShandong Academy of Agricultural Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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 Δcel1a strain independently of its reductive metabolism, but not in the Δcel1a Δcel1b strain. A further comparison of the transcriptional responses of the Δcel1a Δcel1b strain complemented with wild-type CEL1a or a catalytically inactive CEL1a version and the Δcel1a 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.

Indexed as

beta-GlucosidaseCellulaseEnzyme InductionFungal ProteinsGalactoseGene Knockout TechniquesHydrolysisIntracellular FluidLactoseTranscription, GeneticTrichodermabeta-GlucosidaseCellulaseFungal ProteinsGalactoseLactose

Identifiers

PMID24879125
PMCPMC4135799
OpenAlexW2158903967

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.