Three regulators of G protein signaling differentially affect mating, morphology and virulence in the smut fungus Ustilago maydis. Issue 6 (21st July 2017)
- Record Type:
- Journal Article
- Title:
- Three regulators of G protein signaling differentially affect mating, morphology and virulence in the smut fungus Ustilago maydis. Issue 6 (21st July 2017)
- Main Title:
- Three regulators of G protein signaling differentially affect mating, morphology and virulence in the smut fungus Ustilago maydis
- Authors:
- Moretti, Marino
Wang, Lei
Grognet, Pierre
Lanver, Daniel
Link, Hannes
Kahmann, Regine - Abstract:
- Summary: Regulators of G protein signaling (RGS) proteins modulate heterotrimeric G protein signaling negatively. To broaden an understanding of the roles of RGS proteins in fungal pathogens, we functionally characterized the three RGS protein‐encoding genes ( rgs1, rgs2 and rgs3 ) in the phytopathogenic fungus Ustilago maydis . It was found that RGS proteins played distinct roles in the regulation of development and virulence. rgs1 had a minor role in virulence when deleted in a solopathogenic strain. In crosses, rgs1 was dispensable for mating and filamentation, but was required for teliospore production. Haploid rgs2 mutants were affected in cell morphology, growth, mating and were unable to cause disease symptoms in crosses. However, virulence was unaffected when rgs2 was deleted in a solopathogenic strain, suggesting an exclusive involvement in pre‐fusion events. These rgs2 phenotypes are likely connected to elevated intracellular cAMP levels. rgs3 mutants were severely attenuated in mating, in their response to pheromone, virulence and formation of mature teliospores. The mating defect could be traced back to reduced expression of the transcription factor rop1 . It was speculated that the distinct roles of the three U. maydis RGS proteins were achieved by direct modulation of the Gα subunit‐activated signaling pathways as well as through Gα‐independent functions. Abstract : RGS proteins are important regulators of G protein signaling via their interaction withSummary: Regulators of G protein signaling (RGS) proteins modulate heterotrimeric G protein signaling negatively. To broaden an understanding of the roles of RGS proteins in fungal pathogens, we functionally characterized the three RGS protein‐encoding genes ( rgs1, rgs2 and rgs3 ) in the phytopathogenic fungus Ustilago maydis . It was found that RGS proteins played distinct roles in the regulation of development and virulence. rgs1 had a minor role in virulence when deleted in a solopathogenic strain. In crosses, rgs1 was dispensable for mating and filamentation, but was required for teliospore production. Haploid rgs2 mutants were affected in cell morphology, growth, mating and were unable to cause disease symptoms in crosses. However, virulence was unaffected when rgs2 was deleted in a solopathogenic strain, suggesting an exclusive involvement in pre‐fusion events. These rgs2 phenotypes are likely connected to elevated intracellular cAMP levels. rgs3 mutants were severely attenuated in mating, in their response to pheromone, virulence and formation of mature teliospores. The mating defect could be traced back to reduced expression of the transcription factor rop1 . It was speculated that the distinct roles of the three U. maydis RGS proteins were achieved by direct modulation of the Gα subunit‐activated signaling pathways as well as through Gα‐independent functions. Abstract : RGS proteins are important regulators of G protein signaling via their interaction with GTP‐bound Gα subunits. Rgs1, Rgs2 and Rgs3 of the maize pathogen Ustilago maydis have been functionally characterized. We show that these RGS proteins have distinct functions in maintenance of cell shape, mating, teliospore development and virulence. … (more)
- Is Part Of:
- Molecular microbiology. Volume 105:Issue 6(2017)
- Journal:
- Molecular microbiology
- Issue:
- Volume 105:Issue 6(2017)
- Issue Display:
- Volume 105, Issue 6 (2017)
- Year:
- 2017
- Volume:
- 105
- Issue:
- 6
- Issue Sort Value:
- 2017-0105-0006-0000
- Page Start:
- 901
- Page End:
- 921
- Publication Date:
- 2017-07-21
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.13745 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 4579.xml