%0 Journal Article %1 Pott:2000:Fungal-Genet-Biol:11118135 %A Pott, G B %A Miller, T K %A Bartlett, J A %A Palas, J S %A Selitrennikoff, C P %D 2000 %J Fungal Genet Biol %K phosphorelay %N 1 %P 55-67 %R 10.1006/fgbi.2000.1225 %T The isolation of FOS-1, a gene encoding a putative two-component histidine kinase from Aspergillus fumigatus %U http://www.ncbi.nlm.nih.gov/pubmed/11118135?dopt=Abstract %V 31 %X In fungi, two-component histidine kinases are involved in response mechanisms to extracellular changes in osmolarity, resistance to dicarboximide fungicides, and cell-wall assembly. In the human opportunistic fungus, Candida albicans, each of the three histidine kinases plays a role in virulence. Here, we identify, for the first time, a gene, FOS-1, from the human pathogenic fungus Aspergillus fumigatus that predicts a protein with homology to two-component histidine kinases. The predicted FOS-1 protein is highly homologous to bacterial and other fungal histidine kinases in several functional domains, but is divergent at the amino- and carboxy-termini. A mutant lacking the FOS-1 locus, DeltaFOS-1, did not exhibit a detectable defect in either hyphal growth or morphology when grown on solid or liquid medium. However, in liquid medium, conidiophore development of the DeltaFOS-1 mutant was delayed. Compared to wild type, the DeltaFOS-1 strain was neither osmotically sensitive nor sensitive or resistant to a number of nondicarboximide antifungal drugs, but was highly resistant to dicarboximide fungicides and resistant to novozym 234, suggesting that FOS-1p may play a role in the regulation of cell-wall assembly.

@article{Pott:2000:Fungal-Genet-Biol:11118135, abstract = {In fungi, two-component histidine kinases are involved in response mechanisms to extracellular changes in osmolarity, resistance to dicarboximide fungicides, and cell-wall assembly. In the human opportunistic fungus, Candida albicans, each of the three histidine kinases plays a role in virulence. Here, we identify, for the first time, a gene, FOS-1, from the human pathogenic fungus Aspergillus fumigatus that predicts a protein with homology to two-component histidine kinases. The predicted FOS-1 protein is highly homologous to bacterial and other fungal histidine kinases in several functional domains, but is divergent at the amino- and carboxy-termini. A mutant lacking the FOS-1 locus, DeltaFOS-1, did not exhibit a detectable defect in either hyphal growth or morphology when grown on solid or liquid medium. However, in liquid medium, conidiophore development of the DeltaFOS-1 mutant was delayed. Compared to wild type, the DeltaFOS-1 strain was neither osmotically sensitive nor sensitive or resistant to a number of nondicarboximide antifungal drugs, but was highly resistant to dicarboximide fungicides and resistant to novozym 234, suggesting that FOS-1p may play a role in the regulation of cell-wall assembly.}, added-at = {2008-12-13T17:51:07.000+0100}, author = {Pott, G B and Miller, T K and Bartlett, J A and Palas, J S and Selitrennikoff, C P}, biburl = {https://www.bibsonomy.org/bibtex/27dce25c439404ef6c9de321c4e7fdb83/ben8bibsonomy}, description = {The isolation of FOS-1, a gene encoding a putative...[Fungal Genet Biol. 2000] - PubMed Result}, doi = {10.1006/fgbi.2000.1225}, interhash = {ac31de5021e97f536038a420cd4da38a}, intrahash = {7dce25c439404ef6c9de321c4e7fdb83}, journal = {Fungal Genet Biol}, keywords = {phosphorelay}, month = Oct, number = 1, pages = {55-67}, pmid = {11118135}, timestamp = {2008-12-13T17:51:07.000+0100}, title = {The isolation of FOS-1, a gene encoding a putative two-component histidine kinase from Aspergillus fumigatus}, url = {http://www.ncbi.nlm.nih.gov/pubmed/11118135?dopt=Abstract}, volume = 31, year = 2000 }