In three putative histidine kinase genes have been described thus far, including and . The encoded proteins for CaSln 1p and CaNik 1p, which are similar to Sln 1p from and Nik-1 from seem to function in osmoregulation and morphogenesis, respectively. Recently, the isolation of a putative histidine kinase gene from has been reported. In addition to the histidine and aspartyl domains located at its C-terminus as previously described, it is shown here that the N-terminal domain of Cahk 1p contains a P-loop motif and a sequence which shows significant homology with the seven C-terminal domains of serine/threonine kinases. The Ser/Thrhomologous domains of Cahk 1p could, in fact, correspond to its sensor sequence. has been mapped to chromosome 2 and gene deletion studies were undertaken to understand its function. Δ mutants are phenotypically different from any other histidine kinase mutants thus far described either in or in any other yeast or filamentous fungus. This study demonstrates that Δ mutants flocculate extensively in a gene-dosage-dependent manner under conditions which induce germ-tube formation, such as growth in medium 199 (pH 7·5). The flocculation occurs by an interaction along the hyphal surfaces, probably because of the altered expression of one or more hyphal-cell-surface components in the Δ mutants. These results indicate that could be involved in regulating their expression.


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