Deletion of the HAMP domains from the histidine kinase CaNik1p of Candida albicans or treatment with fungicides activates the MAP kinase Hog1p in S. cerevisiae transformants.

2.50
Hdl Handle:
http://hdl.handle.net/10033/305074
Title:
Deletion of the HAMP domains from the histidine kinase CaNik1p of Candida albicans or treatment with fungicides activates the MAP kinase Hog1p in S. cerevisiae transformants.
Authors:
El-Mowafy, Mohammed; Bahgat, Mahmoud M; Bilitewski, Ursula
Abstract:
Microorganisms use two-component signal transduction (TCST) systems to regulate the response of the organism to changes of environmental conditions. Such systems are absent from mammalian cells and are thus of interest as drug targets. Fungal TCST systems are usually composed of a hybrid histidine kinase, comprising the histidine kinase (HisKA) domain and a receiver domain, a histidine phosphotransfer protein and a response regulator. Among the 11 groups of fungal histidine kinases, group III histidine kinases are of particular relevance as they are essential for the activity of different groups of fungicides. A characteristic feature is the N-terminal amino acid repeat domain comprising multiple HAMP domains, of which the function is still largely unknown. In Candida albicans, a fungal human pathogen, three histidine kinases were identified, of which CaNik1p is a group III histidine kinase. Heterologous expression of this protein in Sacchromyces cerevisiae conferred susceptibility to different fungicides. Fungicide activity was associated with phosphorylation of the mitogen activated protein kinase Hog1p.
Citation:
Deletion of the HAMP domains from the histidine kinase CaNik1p of Candida albicans or treatment with fungicides activates the MAP kinase Hog1p in S. cerevisiae transformants. 2013, 13 (1):209 BMC Microbiol.
Journal:
BMC microbiology
Issue Date:
17-Sep-2013
URI:
http://hdl.handle.net/10033/305074
DOI:
10.1186/1471-2180-13-209
PubMed ID:
24044701
Type:
Article
ISSN:
1471-2180
Appears in Collections:
publications of the research group compound profiling and screening (COPS)

Full metadata record

DC FieldValue Language
dc.contributor.authorEl-Mowafy, Mohammeden
dc.contributor.authorBahgat, Mahmoud Men
dc.contributor.authorBilitewski, Ursulaen
dc.date.accessioned2013-11-07T12:05:13Z-
dc.date.available2013-11-07T12:05:13Z-
dc.date.issued2013-09-17-
dc.identifier.citationDeletion of the HAMP domains from the histidine kinase CaNik1p of Candida albicans or treatment with fungicides activates the MAP kinase Hog1p in S. cerevisiae transformants. 2013, 13 (1):209 BMC Microbiol.en
dc.identifier.issn1471-2180-
dc.identifier.pmid24044701-
dc.identifier.doi10.1186/1471-2180-13-209-
dc.identifier.urihttp://hdl.handle.net/10033/305074-
dc.description.abstractMicroorganisms use two-component signal transduction (TCST) systems to regulate the response of the organism to changes of environmental conditions. Such systems are absent from mammalian cells and are thus of interest as drug targets. Fungal TCST systems are usually composed of a hybrid histidine kinase, comprising the histidine kinase (HisKA) domain and a receiver domain, a histidine phosphotransfer protein and a response regulator. Among the 11 groups of fungal histidine kinases, group III histidine kinases are of particular relevance as they are essential for the activity of different groups of fungicides. A characteristic feature is the N-terminal amino acid repeat domain comprising multiple HAMP domains, of which the function is still largely unknown. In Candida albicans, a fungal human pathogen, three histidine kinases were identified, of which CaNik1p is a group III histidine kinase. Heterologous expression of this protein in Sacchromyces cerevisiae conferred susceptibility to different fungicides. Fungicide activity was associated with phosphorylation of the mitogen activated protein kinase Hog1p.en
dc.languageENG-
dc.rightsArchived with thanks to BMC microbiologyen
dc.titleDeletion of the HAMP domains from the histidine kinase CaNik1p of Candida albicans or treatment with fungicides activates the MAP kinase Hog1p in S. cerevisiae transformants.-
dc.typeArticleen
dc.identifier.journalBMC microbiologyen

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