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Deletion of the col-26 Transcription Factor Gene and a Point Mutation in the exo-1 F-Box Protein Gene Confer Sorbose Resistance in Neurospora crassa
L-Sorbose induces hyperbranching of hyphae, which results in colonial growth in Neurospora crassa. The sor-4 gene, which encodes a glucose sensor that acts in carbon catabolite repression (CCR), has been identified as a sorbose resistance gene. In this study, we found that the deletion mutant of col...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9697653/ https://www.ncbi.nlm.nih.gov/pubmed/36354936 http://dx.doi.org/10.3390/jof8111169 |
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author | Hirai, Kenshi Idemoto, Takuya Kato, Shiho Ichiishi, Akihiko Fukumori, Fumiyasu Fujimura, Makoto |
author_facet | Hirai, Kenshi Idemoto, Takuya Kato, Shiho Ichiishi, Akihiko Fukumori, Fumiyasu Fujimura, Makoto |
author_sort | Hirai, Kenshi |
collection | PubMed |
description | L-Sorbose induces hyperbranching of hyphae, which results in colonial growth in Neurospora crassa. The sor-4 gene, which encodes a glucose sensor that acts in carbon catabolite repression (CCR), has been identified as a sorbose resistance gene. In this study, we found that the deletion mutant of col-26, which encodes an AmyR-like transcription factor that acts in CCR, displayed sorbose resistance. In contrast, the deletion mutants of other CCR genes, such as a hexokinase (hxk-2), an AMP-activated S/T protein kinase (prk-10), and a transcription factor (cre-1), showed no sorbose resistance. Double mutant analysis revealed that the deletion of hxk-2, prk-10, and cre-1 did not affect the sorbose resistance of the col-26 mutant. Genes for a glucoamylase (gla-1), an invertase (inv), and glucose transporters (glt-1 and hgt-1) were highly expressed in the cre-1 mutant, even in glucose-rich conditions, but this upregulation was suppressed in the Δcre-1; Δcol-26a double-deletion mutant. Furthermore, we found that a dgr-2(L1)a mutant with a single amino-acid substitution, S11L, in the F-box protein exo-1 displayed sorbose resistance, unlike the deletion mutants of exo-1, suggesting that the function of exo-1 is crucial for the resistance. Our data strongly suggest that CCR directly participates in sorbose resistance, and that col-26 and exo-1 play important roles in regulating the amylase and glucose transporter genes during CCR. |
format | Online Article Text |
id | pubmed-9697653 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-96976532022-11-26 Deletion of the col-26 Transcription Factor Gene and a Point Mutation in the exo-1 F-Box Protein Gene Confer Sorbose Resistance in Neurospora crassa Hirai, Kenshi Idemoto, Takuya Kato, Shiho Ichiishi, Akihiko Fukumori, Fumiyasu Fujimura, Makoto J Fungi (Basel) Article L-Sorbose induces hyperbranching of hyphae, which results in colonial growth in Neurospora crassa. The sor-4 gene, which encodes a glucose sensor that acts in carbon catabolite repression (CCR), has been identified as a sorbose resistance gene. In this study, we found that the deletion mutant of col-26, which encodes an AmyR-like transcription factor that acts in CCR, displayed sorbose resistance. In contrast, the deletion mutants of other CCR genes, such as a hexokinase (hxk-2), an AMP-activated S/T protein kinase (prk-10), and a transcription factor (cre-1), showed no sorbose resistance. Double mutant analysis revealed that the deletion of hxk-2, prk-10, and cre-1 did not affect the sorbose resistance of the col-26 mutant. Genes for a glucoamylase (gla-1), an invertase (inv), and glucose transporters (glt-1 and hgt-1) were highly expressed in the cre-1 mutant, even in glucose-rich conditions, but this upregulation was suppressed in the Δcre-1; Δcol-26a double-deletion mutant. Furthermore, we found that a dgr-2(L1)a mutant with a single amino-acid substitution, S11L, in the F-box protein exo-1 displayed sorbose resistance, unlike the deletion mutants of exo-1, suggesting that the function of exo-1 is crucial for the resistance. Our data strongly suggest that CCR directly participates in sorbose resistance, and that col-26 and exo-1 play important roles in regulating the amylase and glucose transporter genes during CCR. MDPI 2022-11-06 /pmc/articles/PMC9697653/ /pubmed/36354936 http://dx.doi.org/10.3390/jof8111169 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Hirai, Kenshi Idemoto, Takuya Kato, Shiho Ichiishi, Akihiko Fukumori, Fumiyasu Fujimura, Makoto Deletion of the col-26 Transcription Factor Gene and a Point Mutation in the exo-1 F-Box Protein Gene Confer Sorbose Resistance in Neurospora crassa |
title | Deletion of the col-26 Transcription Factor Gene and a Point Mutation in the exo-1 F-Box Protein Gene Confer Sorbose Resistance in Neurospora crassa |
title_full | Deletion of the col-26 Transcription Factor Gene and a Point Mutation in the exo-1 F-Box Protein Gene Confer Sorbose Resistance in Neurospora crassa |
title_fullStr | Deletion of the col-26 Transcription Factor Gene and a Point Mutation in the exo-1 F-Box Protein Gene Confer Sorbose Resistance in Neurospora crassa |
title_full_unstemmed | Deletion of the col-26 Transcription Factor Gene and a Point Mutation in the exo-1 F-Box Protein Gene Confer Sorbose Resistance in Neurospora crassa |
title_short | Deletion of the col-26 Transcription Factor Gene and a Point Mutation in the exo-1 F-Box Protein Gene Confer Sorbose Resistance in Neurospora crassa |
title_sort | deletion of the col-26 transcription factor gene and a point mutation in the exo-1 f-box protein gene confer sorbose resistance in neurospora crassa |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9697653/ https://www.ncbi.nlm.nih.gov/pubmed/36354936 http://dx.doi.org/10.3390/jof8111169 |
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