Identification of VdASP F2‐interacting protein as a regulator of microsclerotial formation in Verticillium dahliae. Issue 7 (27th April 2022)
- Record Type:
- Journal Article
- Title:
- Identification of VdASP F2‐interacting protein as a regulator of microsclerotial formation in Verticillium dahliae. Issue 7 (27th April 2022)
- Main Title:
- Identification of VdASP F2‐interacting protein as a regulator of microsclerotial formation in Verticillium dahliae
- Authors:
- Guo, Cuimei
Yang, Xing
Shi, Hongli
Chen, Chi
Hu, Zhijuan
Zheng, Xinyao
Yang, Xingyong
Xie, Chengjian - Abstract:
- Summary: Verticillium dahliae, a notorious phytopathogenic fungus, causes vascular wilt diseases in many plant species. The melanized microsclerotia enable V. dahliae to survive for years in soil and are crucial for its disease cycle. In a previous study, we characterized the secretory protein VdASP F2 from V. dahliae and found that VdASP F2 deletion significantly affected the formation of microsclerotia under adverse environmental conditions. In this study, we clarified that VdASP F2 is localized to the cell wall. However, the underlying mechanism of VdASP F2 in microsclerotial formation remains unclear. Transmembrane ion channel protein VdTRP was identified as a candidate protein that interacts with VdASP F2 using pull‐down assays followed by liquid chromatography‐tandem mass spectrometry (LC‐MS/MS) analysis, and interaction of VdASP F2 and VdTRP was confirmed by bimolecular fluorescence complementary and coimmunoprecipitation assays. The deletion mutant was analysed to reveal that VdTRP is required for microsclerotial production, but it is not essential for stress resistance, carbon utilization and pathogenicity of V. dahliae . RNA‐seq revealed some differentially expressed genes related to melanin synthesis and microsclerotial formation were significantly downregulated in the VdTRP deletion mutants. Taken together, these results indicate that VdASP F2 regulates the formation of melanized microsclerotia by interacting with VdTRP. Abstract : VdASP F2 regulates theSummary: Verticillium dahliae, a notorious phytopathogenic fungus, causes vascular wilt diseases in many plant species. The melanized microsclerotia enable V. dahliae to survive for years in soil and are crucial for its disease cycle. In a previous study, we characterized the secretory protein VdASP F2 from V. dahliae and found that VdASP F2 deletion significantly affected the formation of microsclerotia under adverse environmental conditions. In this study, we clarified that VdASP F2 is localized to the cell wall. However, the underlying mechanism of VdASP F2 in microsclerotial formation remains unclear. Transmembrane ion channel protein VdTRP was identified as a candidate protein that interacts with VdASP F2 using pull‐down assays followed by liquid chromatography‐tandem mass spectrometry (LC‐MS/MS) analysis, and interaction of VdASP F2 and VdTRP was confirmed by bimolecular fluorescence complementary and coimmunoprecipitation assays. The deletion mutant was analysed to reveal that VdTRP is required for microsclerotial production, but it is not essential for stress resistance, carbon utilization and pathogenicity of V. dahliae . RNA‐seq revealed some differentially expressed genes related to melanin synthesis and microsclerotial formation were significantly downregulated in the VdTRP deletion mutants. Taken together, these results indicate that VdASP F2 regulates the formation of melanized microsclerotia by interacting with VdTRP. Abstract : VdASP F2 regulates the formation of melanized microsclerotia by interacting with VdTRP in Verticillium dahliae . … (more)
- Is Part Of:
- Microbial biotechnology. Volume 15:Issue 7(2022)
- Journal:
- Microbial biotechnology
- Issue:
- Volume 15:Issue 7(2022)
- Issue Display:
- Volume 15, Issue 7 (2022)
- Year:
- 2022
- Volume:
- 15
- Issue:
- 7
- Issue Sort Value:
- 2022-0015-0007-0000
- Page Start:
- 2040
- Page End:
- 2054
- Publication Date:
- 2022-04-27
- Subjects:
- Microbial biotechnology -- Periodicals
Biotechnology
Microbiology
660.62 - Journal URLs:
- http://ejournals.ebsco.com/direct.asp?JournalID=714890 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1751-7915 ↗
http://www.blackwellpublishing.com/mbt_enhanced/aims.asp ↗
http://www3.interscience.wiley.com/journal/118902527/home ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/1751-7915.14066 ↗
- Languages:
- English
- ISSNs:
- 1751-7915
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5756.911050
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 22969.xml