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The transmembrane protein AaSho1 is essential for appressorium formation and secondary metabolism but dispensable for vegetative growth in pear fungal Alternaria alternata
Year:
2022
Source of publication :
Fungal Biology
Authors :
פרוסקי, דב
;
.
Volume :
126
Co-Authors:

Yongxiang Liu
Yongcai Li
Li Ma
Huiwen Deng
Yi Huang
Qianqian Jiang
Yangyang Yang
Yang Bi
Dov B. Prusky

Facilitators :
From page:
139
To page:
148
(
Total pages:
10
)
Abstract:

The high-osmolarity glycerol response (HOG) pathway is pivotal in environmental stress response, differentiation and virulence of Alternaria alternata. The synthetic high osmolarity sensitive sensor Sho1 has been postulated to regulate the HOG pathway. To determine the regulatory role of transmembrane protein Sho1 on vegetative growth, secondary metabolism and infection structure formation, a gene (AaSho1) encoding Sho1 was cloned and characterized from A. alternata (JT-03). Sequence analysis showed that AaSho1 has all four characteristic transmembrane domains and the SH3 domain present in another Sho1 gene from several filamentous fungal. The quantitative RT-PCR analysis showed that fruit wax extract significantly up-regulated AaSho1 gene expression in vitro. Pharmacological experiments showed that A. alternata treated with nystatin, a specific AaSho1 inhibitor, had no significant effect on the morphology of A. alternata and the invasive growth in pear fruit. However, nystatin treatment significantly reduced spore germination rates on different wax-coated hydrophobic surfaces, with 58.00, 46.70 and 83.72% reduced for fruit wax, beeswax and paraffin coated. Meanwhile, the secondary metabolism altenuene (ALT), tentoxin (TEN) toxin, and melanin content were also affected by nystatin treatment. These findings suggest that AaSho1 is required for the infection structure differentiation and secondary metabolism of A. alternata in response to physiochemical signals on the host surfaces.

Note:
Related Files :
AaSho1
Alternaria alternata
infection structures
nystatin
Secondary metabolism
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.funbio.2021.11.006
Article number:
0
Affiliations:
Database:
סקופוס
Publication Type:
מאמר בדפוס
;
.
Language:
אנגלית
Editors' remarks:
ID:
57288
Last updated date:
16/03/2022 12:49
Creation date:
22/12/2021 14:21
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Scientific Publication
The transmembrane protein AaSho1 is essential for appressorium formation and secondary metabolism but dispensable for vegetative growth in pear fungal Alternaria alternata
126

Yongxiang Liu
Yongcai Li
Li Ma
Huiwen Deng
Yi Huang
Qianqian Jiang
Yangyang Yang
Yang Bi
Dov B. Prusky

The transmembrane protein AaSho1 is essential for appressorium formation and secondary metabolism but dispensable for vegetative growth in pear fungal Alternaria alternata

The high-osmolarity glycerol response (HOG) pathway is pivotal in environmental stress response, differentiation and virulence of Alternaria alternata. The synthetic high osmolarity sensitive sensor Sho1 has been postulated to regulate the HOG pathway. To determine the regulatory role of transmembrane protein Sho1 on vegetative growth, secondary metabolism and infection structure formation, a gene (AaSho1) encoding Sho1 was cloned and characterized from A. alternata (JT-03). Sequence analysis showed that AaSho1 has all four characteristic transmembrane domains and the SH3 domain present in another Sho1 gene from several filamentous fungal. The quantitative RT-PCR analysis showed that fruit wax extract significantly up-regulated AaSho1 gene expression in vitro. Pharmacological experiments showed that A. alternata treated with nystatin, a specific AaSho1 inhibitor, had no significant effect on the morphology of A. alternata and the invasive growth in pear fruit. However, nystatin treatment significantly reduced spore germination rates on different wax-coated hydrophobic surfaces, with 58.00, 46.70 and 83.72% reduced for fruit wax, beeswax and paraffin coated. Meanwhile, the secondary metabolism altenuene (ALT), tentoxin (TEN) toxin, and melanin content were also affected by nystatin treatment. These findings suggest that AaSho1 is required for the infection structure differentiation and secondary metabolism of A. alternata in response to physiochemical signals on the host surfaces.

Scientific Publication
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