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Fungal X-Intrinsic Protein Aquaporin from Trichoderma atroviride: Structural and Functional Considerations

Ben Amira, Maroua and Faize, Mohamed and Karlsson, Magnus and Dubey, Mukesh and Frac, Magdalena and Panek, Jacek and Fumanal, Boris and Gousset-Dupont, Aurelie and Julien, Jean-Louis and Chaar, Hatem and Auguin, Daniel and Mom, Robin and Label, Philippe and Venisse, Jean-Stephane (2021). Fungal X-Intrinsic Protein Aquaporin from Trichoderma atroviride: Structural and Functional Considerations. Biomolecules. 11 , 338
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Abstract

The major intrinsic protein (MIP) superfamily is a key part of the fungal transmembrane transport network. It facilitates the transport of water and low molecular weight solutes across biomembranes. The fungal uncharacterized X-Intrinsic Protein (XIP) subfamily includes the full protein diversity of MIP. Their biological functions still remain fully hypothetical. The aim of this study is still to deepen the diversity and the structure of the XIP subfamily in light of the MIP counterparts-the aquaporins (AQPs) and aquaglyceroporins (AQGPs)-and to describe for the first time their function in the development, biomass accumulation, and mycoparasitic aptitudes of the fungal bioagent Trichoderma atroviride. The fungus-XIP Glade, with one member (TriatXIP), is one of the three clades of MIPs that make up the diversity of T. atroviride MIPs, along with the AQPs (three members) and the AQGPs (three members). TriatXIP resembles those of strict aquaporins, predicting water diffusion and possibly other small polar solutes due to particularly wider ar/R constriction with a Lysine substitution at the LE2 position. The XIP loss of function in Delta TriatXIP mutants slightly delays biomass accumulation but does not impact mycoparasitic activities. Delta TriatMIP forms colonies similar to wild type; however, the hyphae are slightly thinner and colonies produce rare chlamydospores in PDA and specific media, most of which are relatively small and exhibit abnormal morphologies. To better understand the molecular causes of these deviant phenotypes, a wide-metabolic survey of the ATriatXIPs demonstrates that the delayed growth kinetic, correlated to a decrease in respiration rate, is caused by perturbations in the pentose phosphate pathway. Furthermore, the null expression of the XIP gene strongly impacts the expression of four expressed MIP-encoding genes of T. atroviride, a plausible compensating effect which safeguards the physiological integrity and life cycle of the fungus. This paper offers an overview of the fungal XIP family in the biocontrol agent T. atroviride which will be useful for further functional analysis of this particular MIP subfamily in vegetative growth and the environmental stress response in fungi. Ultimately, these findings have implications for the ecophysiology of Trichoderma spp. in natural, agronomic, and industrial systems.

Authors/Creators:Ben Amira, Maroua and Faize, Mohamed and Karlsson, Magnus and Dubey, Mukesh and Frac, Magdalena and Panek, Jacek and Fumanal, Boris and Gousset-Dupont, Aurelie and Julien, Jean-Louis and Chaar, Hatem and Auguin, Daniel and Mom, Robin and Label, Philippe and Venisse, Jean-Stephane
Title:Fungal X-Intrinsic Protein Aquaporin from Trichoderma atroviride: Structural and Functional Considerations
Series Name/Journal:Biomolecules
Year of publishing :2021
Volume:11
Article number:338
Number of Pages:27
Publisher:MDPI
ISSN:2218-273X
Language:English
Publication Type:Journal article
Article category:Scientific peer reviewed
Version:Published version
Copyright:Creative Commons: Attribution 4.0
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Biochemistry and Molecular Biology
Keywords:aquaporin, uncharacterized X-Intrinsic proteins, Trichoderma atroviride, 3D modeling, chlamydospores, pentose phosphate pathway, stress responses
URN:NBN:urn:nbn:se:slu:epsilon-p-111126
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-111126
Additional ID:
Type of IDID
DOI10.3390/biom11020338
Web of Science (WoS)000622159800001
ID Code:22815
Faculty:NJ - Fakulteten för naturresurser och jordbruksvetenskap
Department:(NL, NJ) > Dept. of Forest Mycology and Plant Pathology
(S) > Dept. of Forest Mycology and Plant Pathology
Deposited By: SLUpub Connector
Deposited On:22 Mar 2021 09:03
Metadata Last Modified:22 Mar 2021 09:11

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