We here report the identification of the previously uncharacterized SGD1 gene, encoding a 102.8-kDa protein containing a leucine zipper region and a bipartite nuclear localization signal. Deletion of SGD1 results in loss of cell viability, while an increased dosage of SGD1 partially suppresses the osmosensitivity of pbs2Δ and hog1Δ mutants that are defective in the osmosignaling high osmolarity glycerol (HOG) mitogen-activated protein kinase pathway. The rescued mutants display a partially re-established transcriptional control of the osmostress-induced expression of GPD1, a target gene of the HOG pathway encoding NAD+-dependent glycerol 3-phosphate dehydrogenase, and a partially recovered hyperosmolarity-induced production of glycerol. Consistent with Sgd1p affecting the transcriptional control of GPD1, a functional green fluorescent protein tagged Sgd1p is localized to the cell nucleus.
