High impact information on ZDS1

• Zds1 (also known as Oss1 and Hst1) is important in repressing the transcription of SWE1 in G2 phase [1].
• In the presence of high calcium levels, cells lacking Zds1 are delayed in entering mitosis [1].
• Altogether, these results suggest that Zds1-mediated cytoplasmic localization of Bcy1 is regulated by carbon source-dependent phosphorylation of cluster II serines, while cluster I acts in a Zds1-independent manner [2].
• Deletion of ZDS2 produced no obvious phenotype, and deletion of ZDS1 produced no obvious phenotype other than a mild effect on cell shape [3].
• A genetic screen for GTPase-activating proteins (GAPs) or other negative regulators of the Rac/Rho family GTPase Cdc42p in Saccharomyces cerevisiae identified ZDS1, a gene encoding a protein of 915 amino acids [3].

Biological context of ZDS1

• The ZDS1 gene was isolated as a multicopy suppressor of the cdc28-1N plasmid loss defect [4].
• Disruption of either ZDS1 or ZDS2 causes only modest phenotypes [4].
• However, a strain with both ZDS1 and ZDS2 disrupted is extremely slowly growing, has marked defects in bud morphology, and shows defects in completing S phase or entering mitosis [4].
• Mutations in the homologous ZDS1 and ZDS2 genes affect cell cycle progression [4].
• As ZDS1 and ZDS2 have recently been identified also by numerous other groups studying a wide range of biological phenomena, the roles of Cdc42p in intracellular signaling may be more diverse than has previously been appreciated [3].

Anatomical context of ZDS1

• An increase dosage of ZDS1, or of genes involved in cell wall assembly and in secretion (RHO1 and SR077, respectively), partially suppresses the sensitivity of rpb4delta cells to high temperature, heat shock and stationary phase [5].
• We proposed that Zds1p associates with the complex formed by Dbp5p, Gfd1p, and nucleoporins at the cytosolic fibrils of the nuclear pore complex and is required for optimal mRNA export [6].
• Overexpression of the C-terminal region of Zds1 induced multi-septa and abnormal zygotes [7].

Associations of ZDS1 with chemical compounds

• The zds1-disrupted strain is sensitive to CaCl2, and this effect is suppressed by the C-terminal region of Zds1 [7].

Physical interactions of ZDS1

• The similarity of this localization to that of Cdc42p suggests that Zds1p may interact directly with Cdc42p [3].
• In vitro binding experiments revealed that Gfd1p and Dbp5p bind directly to the C-terminal part of Zds1p [6].
• Here we reported that Dbp5p and Gfd1p interact with Zds1p, a protein previously identified as a multicopy suppressor in several yeast genetic screens [6].

Other interactions of ZDS1

• Furthermore, two new suppressor genes, ZDS1 and GIC1, were identified [8].
• In addition, ZDS1 and ZDS2 both required the open reading frame encoding the N-terminal 174 amino acids of Sir3p to stabilize short YACs [9].
• In addition, ZDS1 interacted genetically with mutant alleles of genes encoding key factors in mRNA export, including DBP5 and MEX67 [6].
• Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity defects of a yeast eIF5A mutant [8].
• A two-hybrid screen aimed to isolate genes encoding proteins that interact with the Bcy1 N-terminal domain identified Zds1 [2].

References