High impact information on STO1

• Furthermore, we find a genetic relationship between Hmt1p and cap-binding protein 80 (CBP80) [1].
• This conclusion was corroborated by finding an inverse relationship of the CBC1 and SKS1 mRNA levels in normal strains grown under different conditions [2].
• Microarray procedures were used to determine the half-lives of mRNAs from normal and mutant strains, leading to the tentative identification of hundreds of normal mRNAs that were notably stabilized when either CBC1 or RRP6 were deleted [2].
• In this report, we define a genetic relationship between NPL3 and the nonessential genes encoding the subunits of the cap-binding complex (CBP80 and CBP20) [3].
• Further analysis showed that gcr3 mutations also suppressed the temperature-sensitive growth of hpr1 single mutants [4].

Biological context of STO1

• Plasmid DNA isolated from gcr3 mutants was significantly more negatively supercoiled than normal, suggesting that Gcr3 protein, like topoisomerase I and Hpr1p, affects chromatin structure, perhaps during transcription [4].
• The GCR3 gene was obtained by growth complementation from a genomic DNA library, and the complemented strains had normal enzyme levels [5].
• The recessive single nuclear gene mutation, named gcr3, caused an extremely defective growth phenotype on fermentable carbon sources such as glucose, while growth on respiratory media was almost normal [5].

Associations of STO1 with chemical compounds

• Interestingly, the sto1-delta deletion mutant stopped growing earlier than the parent and produced 20% more ethanol from xylose [6].

Regulatory relationships of STO1

• The fact that top1 suppressed the growth defect of gcr3 suggested an interaction between those two genes also [4].

Other interactions of STO1

• Mutations in GCR3, a gene involved in the expression of glycolytic genes in Saccharomyces cerevisiae, suppress the temperature-sensitive growth of hpr1 mutants [4].

Analytical, diagnostic and therapeutic context of STO1

• The resulting sto1-delta deletion mutant, FPL-Shi31, did not contain other isoforms of Sto protein that were detectable by Western blot analysis using an alternative oxidase monoclonal antibody raised against the Sto protein from Sauromatum guttatum [6].

References