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Putative Calcium Channels CchA and MidA Play the Important Roles in Conidiation, Hyphal Polarity and Cell Wall Components in Aspergillus nidulans
Although the high affinity Ca(2+) channel, Cch1, and its subunit Mid1 have been investigated and evaluated in yeast and some of filamentous fungi, little is known about the function of their homologs in the Aspergilli. Here, we have functionally characterized the yeast homologs, CchA and MidA, in As...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3470553/ https://www.ncbi.nlm.nih.gov/pubmed/23071589 http://dx.doi.org/10.1371/journal.pone.0046564 |
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author | Wang, Sha Cao, Jinling Liu, Xiao Hu, Hongqin Shi, Jie Zhang, Shizhu Keller, Nancy P. Lu, Ling |
author_facet | Wang, Sha Cao, Jinling Liu, Xiao Hu, Hongqin Shi, Jie Zhang, Shizhu Keller, Nancy P. Lu, Ling |
author_sort | Wang, Sha |
collection | PubMed |
description | Although the high affinity Ca(2+) channel, Cch1, and its subunit Mid1 have been investigated and evaluated in yeast and some of filamentous fungi, little is known about the function of their homologs in the Aspergilli. Here, we have functionally characterized the yeast homologs, CchA and MidA, in Aspergillus nidulans using conditional and null deletion mutants. CchA and MidA not only have functional benefits of fast growth, which is consistent with Cch1 and Mid1 in yeast, but also have unique and complex roles in regulating conidiation, hyphal polarity and cell wall components in low-calcium environments. The defect of CchA or MidA resulted in a sharp reduction in the number of conidiospores, accompanied by abnormal metulae, and undeveloped-phialides at a higher density of inoculum. Most interestingly, these conidiation defects in mutants can, remarkably, be rescued either by extra-cellular Ca(2+) in a calcineurin-dependent way or by osmotic stress in a calcineurin-independent way. Moreover, the fact that the phenotypic defects are not exacerbated by the presence of the double deletion, together with the Y2H assay, indicates that CchA and MidA may form a complex to function together. Our findings suggest that the high-affinity Ca(2+) channel may represent a viable and completely unexplored avenue to reduce conidiation in the Aspergilli. |
format | Online Article Text |
id | pubmed-3470553 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-34705532012-10-15 Putative Calcium Channels CchA and MidA Play the Important Roles in Conidiation, Hyphal Polarity and Cell Wall Components in Aspergillus nidulans Wang, Sha Cao, Jinling Liu, Xiao Hu, Hongqin Shi, Jie Zhang, Shizhu Keller, Nancy P. Lu, Ling PLoS One Research Article Although the high affinity Ca(2+) channel, Cch1, and its subunit Mid1 have been investigated and evaluated in yeast and some of filamentous fungi, little is known about the function of their homologs in the Aspergilli. Here, we have functionally characterized the yeast homologs, CchA and MidA, in Aspergillus nidulans using conditional and null deletion mutants. CchA and MidA not only have functional benefits of fast growth, which is consistent with Cch1 and Mid1 in yeast, but also have unique and complex roles in regulating conidiation, hyphal polarity and cell wall components in low-calcium environments. The defect of CchA or MidA resulted in a sharp reduction in the number of conidiospores, accompanied by abnormal metulae, and undeveloped-phialides at a higher density of inoculum. Most interestingly, these conidiation defects in mutants can, remarkably, be rescued either by extra-cellular Ca(2+) in a calcineurin-dependent way or by osmotic stress in a calcineurin-independent way. Moreover, the fact that the phenotypic defects are not exacerbated by the presence of the double deletion, together with the Y2H assay, indicates that CchA and MidA may form a complex to function together. Our findings suggest that the high-affinity Ca(2+) channel may represent a viable and completely unexplored avenue to reduce conidiation in the Aspergilli. Public Library of Science 2012-10-12 /pmc/articles/PMC3470553/ /pubmed/23071589 http://dx.doi.org/10.1371/journal.pone.0046564 Text en © 2012 Wang et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Wang, Sha Cao, Jinling Liu, Xiao Hu, Hongqin Shi, Jie Zhang, Shizhu Keller, Nancy P. Lu, Ling Putative Calcium Channels CchA and MidA Play the Important Roles in Conidiation, Hyphal Polarity and Cell Wall Components in Aspergillus nidulans |
title | Putative Calcium Channels CchA and MidA Play the Important Roles in Conidiation, Hyphal Polarity and Cell Wall Components in Aspergillus nidulans
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title_full | Putative Calcium Channels CchA and MidA Play the Important Roles in Conidiation, Hyphal Polarity and Cell Wall Components in Aspergillus nidulans
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title_fullStr | Putative Calcium Channels CchA and MidA Play the Important Roles in Conidiation, Hyphal Polarity and Cell Wall Components in Aspergillus nidulans
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title_full_unstemmed | Putative Calcium Channels CchA and MidA Play the Important Roles in Conidiation, Hyphal Polarity and Cell Wall Components in Aspergillus nidulans
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title_short | Putative Calcium Channels CchA and MidA Play the Important Roles in Conidiation, Hyphal Polarity and Cell Wall Components in Aspergillus nidulans
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title_sort | putative calcium channels ccha and mida play the important roles in conidiation, hyphal polarity and cell wall components in aspergillus nidulans |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3470553/ https://www.ncbi.nlm.nih.gov/pubmed/23071589 http://dx.doi.org/10.1371/journal.pone.0046564 |
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