ArticleFEMS yeast research2016
Extended N-terminal region of the essential phosphorelay signaling protein Ypd1 from Cryptococcus neoformans contributes to structural stability, phosphostability and binding of calcium ions.
Article in FEMS yeast research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Signaling Pathways Regulating Dimorphism in Medically Relevant Fungal Species.Pathogens (Basel, Switzerland) · 2025Review
- Structural and functional insights underlying recognition of histidine phosphotransfer protein in fungal phosphorelay systems.Communications biology · 2024Article
- Genetic Analysis Reveals a Requirement for the Hybrid Sensor Kinase RscS inJournal of bacteriology · 2023Article
- A frameshift ineLife · 2023Article
- Predicted Functional and Structural Diversity of Receiver Domains in Fungal Two-Component Regulatory Systems.mSphere · 2021Article
- A Radical Reimagining of Fungal Two-Component Regulatory Systems.Trends in microbiology · 2021Review
- The phosphorelay signal transduction system in Candida glabrata: an in silico analysis.Journal of molecular modeling · 2017Article
- The yeasts phosphorelay systems: a comparative view.World journal of microbiology & biotechnology · 2017Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Rapid response to external stimuli is crucial for survival and proliferation of microorganisms. Pathogenic fungi employ histidine-to-aspartate multistep phosphorelay systems to respond to environmental stress, progress through developmental stages and to produce virulence factors. Because these His-to-Asp phosphorelay systems are not found in humans, they are potential targets for the development of new antifungal therapies. Here we report the characterization of the histidine phosphotransfer (HPt) protein Ypd1 from the human fungal pathogen Cryptococcus neoformans Results from this study demonstrate that CnYpd1 indeed functions as a phosphorelay protein in vitro, and that H138 is confirmed as the site of phosphorylation. We found that CnYpd1 exhibits unique characteristics in comparison to other histidine phosphotransfer proteins, such as an extended N-terminal amino acid sequence, which we find contributes to structural integrity, a longer phosphorylated life time and the ability to bind calcium ions.
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Registered trials
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