Cloned (Comment) | Organism |
---|---|
AaHSK1 DNA and amino acid sequence determination and analysis, cloning from strain EV-MIL31 | Alternaria alternata |
Protein Variants | Comment | Organism |
---|---|---|
additional information | generation of an enzyme deletion mutant strain by gene disruption of AaHSK1 using a hygromycin phosphotransferase gene (HYG) cassette | Alternaria alternata |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | the enzyme lacks transmembrane domains | Alternaria alternata | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Alternaria alternata | AaHSK1 may interact with AaHOG1 at post-translational levels | ? | - |
? | |
additional information | Alternaria alternata EV-MIL31 | AaHSK1 may interact with AaHOG1 at post-translational levels | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alternaria alternata | D3J125 | - |
- |
Alternaria alternata EV-MIL31 | D3J125 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | AaHSK1 may interact with AaHOG1 at post-translational levels | Alternaria alternata | ? | - |
? | |
additional information | AaHSK1 may interact with AaHOG1 at post-translational levels | Alternaria alternata EV-MIL31 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme AaHSK1 has several conserved domains and motifs, such as a HAMP (histidine kinase, adenylate cyclase, methyl binding protein, and phosphatase) domain and a dimerization/phosphoacceptor domain. AaHSK1 contains four repeat domains within HAMP | Alternaria alternata |
Synonyms | Comment | Organism |
---|---|---|
AaHSK1 | - |
Alternaria alternata |
Group III histidine kinase | - |
Alternaria alternata |
Group III HK | - |
Alternaria alternata |
two-component histidine kinase | - |
Alternaria alternata |
General Information | Comment | Organism |
---|---|---|
malfunction | impairment of the AaHSK1 gene does not reduce radial growth of the resulting two null mutants (HD1 and HD2) in the presence of tert-butyl-hydroxyperoxide, H2O2, KCl or NaCl, compared to the wild-type. Expression of a functional copy of the AaHSK1 gene in the HD1 null mutant fully restores the altered phenotypes. Deletion of AaHSK1 affects AaHOG1 phosphorylation. Fungal mutants impaired in AaHSK1, AaHOG1, AaAP1 (encoding a redox-responsive transcription factor) or AaFUS3 (encoding a MAP kinase) are all hypersensitive to 2-chloro-5-hydroxypyridine or 2,3,5-triiodobenzoic acid. Glucose enhances AaHOG1 phosphorylation and nuclear localization in the AaHSK1 deficient background. Genetic disruption of the AaHSK1 gene yields fungal strains that are insensitive to dicarboximide (iprodione and vinclozolin) and phenylpyrrole (fludioxonil) fungicides. Inactivation of the AaHSK1 or AaHOG1 gene does not alter the production of host-selective ACT toxin by Alternaria alternata | Alternaria alternata |
metabolism | the AaHOG1-mediated pathway confers cellular resistance to salts and oxidative stress and bypasses AaHSK1. Accumulation of the AaHSK1 gene transcript is negatively regulated by AaHOG1, AaAP1 or AaFUS3. AaHOG1 is necessary for fungal pathogenicity, yet AaHSK1 is completely dispensable for pathogenicity. AaHSK1 functions in osmotic tolerance without involving AaHOG1. Relationships between the HOG1 MAP kinase and the histidine kinase in Alternaria alternata, overview | Alternaria alternata |
physiological function | AaHSK1 is a primary regulator for cellular resistance to sugar osmotic stress and for sensitivity to dicarboximide or phenylpyrrole fungicides. Important role of AaHSK1 in osmotic adaption, specifically to sugar osmoticants. AaHSK1 does not play an essential role in fungal pathogenicity | Alternaria alternata |