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The anisin1 gene encodes a defensin-like protein and supports the fitness of Aspergillus nidulans
In the genome of Aspergillus nidulans, a defensin-like protein, Anisin1, was annotated with high homology to the mosquito defensin AaDefA1. So far, no studies exist on defensins from filamentous ascomycetes. Therefore, we characterized the anisin1 gene in A. nidulans and generated a deletion mutant,...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer-Verlag
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3354322/ https://www.ncbi.nlm.nih.gov/pubmed/22113351 http://dx.doi.org/10.1007/s00203-011-0773-y |
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author | Eigentler, Andrea Pócsi, István Marx, Florentine |
author_facet | Eigentler, Andrea Pócsi, István Marx, Florentine |
author_sort | Eigentler, Andrea |
collection | PubMed |
description | In the genome of Aspergillus nidulans, a defensin-like protein, Anisin1, was annotated with high homology to the mosquito defensin AaDefA1. So far, no studies exist on defensins from filamentous ascomycetes. Therefore, we characterized the anisin1 gene in A. nidulans and generated a deletion mutant, which suffered from a defect in mitospore development and produced less conidia at 42°C compared to the reference strain. In surface cultures of A. nidulans wild type, the anisin1 expression correlated with that of the central regulator for asexual development, brlA, and with the major scavanger of H(2)O(2) stress, catB, which is indicative for cell differentiation in developing fungi. Interestingly, brlA and anisin1 expressions were deregulated in a ΔsrrA strain that covers a central role in the histidine-to-aspartate (His-Asp) phosphorelay signaling pathway and shows impaired asexual development and H(2)O(2) detoxification. In submers cultures of A. nidulans wild type and other mutants of the His-Asp phosphorelay signaling pathway, anisin1 was repressed, but derepressed in a ΔsrrA background, and anisin1 transcription was further increased in this mutant by H(2)O(2) addition. We therefore conclude that the secreted protein Anisin1 contributes to the optimal development of A. nidulans and we further propose that it has a sensing/signaling function for elevated H(2)O(2) levels. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00203-011-0773-y) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-3354322 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Springer-Verlag |
record_format | MEDLINE/PubMed |
spelling | pubmed-33543222012-05-31 The anisin1 gene encodes a defensin-like protein and supports the fitness of Aspergillus nidulans Eigentler, Andrea Pócsi, István Marx, Florentine Arch Microbiol Original Paper In the genome of Aspergillus nidulans, a defensin-like protein, Anisin1, was annotated with high homology to the mosquito defensin AaDefA1. So far, no studies exist on defensins from filamentous ascomycetes. Therefore, we characterized the anisin1 gene in A. nidulans and generated a deletion mutant, which suffered from a defect in mitospore development and produced less conidia at 42°C compared to the reference strain. In surface cultures of A. nidulans wild type, the anisin1 expression correlated with that of the central regulator for asexual development, brlA, and with the major scavanger of H(2)O(2) stress, catB, which is indicative for cell differentiation in developing fungi. Interestingly, brlA and anisin1 expressions were deregulated in a ΔsrrA strain that covers a central role in the histidine-to-aspartate (His-Asp) phosphorelay signaling pathway and shows impaired asexual development and H(2)O(2) detoxification. In submers cultures of A. nidulans wild type and other mutants of the His-Asp phosphorelay signaling pathway, anisin1 was repressed, but derepressed in a ΔsrrA background, and anisin1 transcription was further increased in this mutant by H(2)O(2) addition. We therefore conclude that the secreted protein Anisin1 contributes to the optimal development of A. nidulans and we further propose that it has a sensing/signaling function for elevated H(2)O(2) levels. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00203-011-0773-y) contains supplementary material, which is available to authorized users. Springer-Verlag 2011-11-24 2012 /pmc/articles/PMC3354322/ /pubmed/22113351 http://dx.doi.org/10.1007/s00203-011-0773-y Text en © The Author(s) 2011 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. |
spellingShingle | Original Paper Eigentler, Andrea Pócsi, István Marx, Florentine The anisin1 gene encodes a defensin-like protein and supports the fitness of Aspergillus nidulans |
title | The anisin1 gene encodes a defensin-like protein and supports the fitness of Aspergillus nidulans |
title_full | The anisin1 gene encodes a defensin-like protein and supports the fitness of Aspergillus nidulans |
title_fullStr | The anisin1 gene encodes a defensin-like protein and supports the fitness of Aspergillus nidulans |
title_full_unstemmed | The anisin1 gene encodes a defensin-like protein and supports the fitness of Aspergillus nidulans |
title_short | The anisin1 gene encodes a defensin-like protein and supports the fitness of Aspergillus nidulans |
title_sort | anisin1 gene encodes a defensin-like protein and supports the fitness of aspergillus nidulans |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3354322/ https://www.ncbi.nlm.nih.gov/pubmed/22113351 http://dx.doi.org/10.1007/s00203-011-0773-y |
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