TPS2 BASIC INFORMATION
| Standard Name | TPS2 |
|---|---|
| Systematic Name | YDR074W |
| Alias | HOG2 , PFK3 |
| Feature Type | ORF, Verified |
| Description | Phosphatase subunit of the trehalose-6-phosphate synthase/phosphatase complex, which synthesizes the storage carbohydrate trehalose; expression is induced by stress conditions and repressed by the Ras-cAMP pathway (1, 2 and see Summary Paragraph)
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| Name Description | Trehalose-6-phosphate PhoSphatase |
| GO Annotations | All TPS2 GO evidence and references |
|---|---|
| View Computational GO annotations for TPS2 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated | |
| High-throughput |
| Pathways |
|---|
| Interactions | TPS2 All interactions details and references |
|---|---|
| 74 total interaction(s) for 59 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000002481 |
|---|
ADDITIONAL INFORMATION for TPS2
SUMMARY PARAGRAPH for TPS2
In Saccharomyces cerevisiae, trehalose is a major reserve carbohydrate involved in reponses to thermal, osmotic, oxidative, and ethanol stresses (3), as well as the suppression of denatured protein aggregation (4). Trehalose biosynthesis is a two-step process in which glucose 6-phosphate and UDP-glucose are converted by trehalose-6-phosphate synthase (TPS), encoded by TPS1, into alpha,alpha-trehalose 6-phosphate, which is then converted with water into trehalose and phosphate by trehalose-6-phosphate phosphatase (TPP), encoded by TPS2 (5). The trehalose biosynthetic pathway can affect glycolysis in that one of its intermediates, trehalose-6-phosphate, inhibits hexokinase activity, which restricts the influx of sugars to glycolysis during the switch to fermentative metabolism (6).
Tps1p and Tps2p are part of the alpha,alpha-trehalose-phosphate synthase complex (7, 2) with Tps3p and Tsl1p, regulatory proteins with partially overlapping functions (8), though some Tps1p appears to be present in the cell as a monomer (9). TPS1, TPS2, TPS3 and TSL1 are coinduced under stress conditions, and corepressed by the Ras-cAMP pathway (1).
Deletion of TPS1 results in loss of both TPS activity and trehalose biosynthesis (7), whereas deletion of TPS2 results in temperature sensitivity and loss of TPP activity (2). Deletion of either TPS1 or TPS2 results in a growth defect on fermentable carbon sources (7, 2). Deletion of either TPS3 or TSL1 has only mild effects, but deletion of both TPS3 and TSL1 results in significant reductions in TPS and TPP activities, as well as reduced trehalose biosynthesis (9).
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for TPS2]
| 1) | Winderickx J, et al. (1996) Regulation of genes encoding subunits of the trehalose synthase complex in Saccharomyces cerevisiae: novel variations of STRE-mediated transcription control? Mol Gen Genet 252(4):470-82 |
| 2) | De Virgilio C, et al. (1993) Disruption of TPS2, the gene encoding the 100-kDa subunit of the trehalose-6-phosphate synthase/phosphatase complex in Saccharomyces cerevisiae, causes accumulation of trehalose-6-phosphate and loss of trehalose-6-phosphate phosphatase activity. Eur J Biochem 212(2):315-23 |
| 3) | Pereira MD, et al. (2001) Acquisition of tolerance against oxidative damage in Saccharomyces cerevisiae. BMC Microbiol 1():11 |
| 4) | Singer MA and Lindquist S (1998) Multiple effects of trehalose on protein folding in vitro and in vivo. Mol Cell 1(5):639-48 |
| 5) | Francois J and Parrou JL (2001) Reserve carbohydrates metabolism in the yeast Saccharomyces cerevisiae. FEMS Microbiol Rev 25(1):125-45 |
| 6) | Hohmann S, et al. (1996) Evidence for trehalose-6-phosphate-dependent and -independent mechanisms in the control of sugar influx into yeast glycolysis. Mol Microbiol 20(5):981-91 |
| 7) | Bell W, et al. (1992) Characterization of the 56-kDa subunit of yeast trehalose-6-phosphate synthase and cloning of its gene reveal its identity with the product of CIF1, a regulator of carbon catabolite inactivation. Eur J Biochem 209(3):951-9 |
| 8) | Vuorio OE, et al. (1993) Cloning of two related genes encoding the 56-kDa and 123-kDa subunits of trehalose synthase from the yeast Saccharomyces cerevisiae. Eur J Biochem 216(3):849-61 |
| 9) | Bell W, et al. (1998) Composition and functional analysis of the Saccharomyces cerevisiae trehalose synthase complex. J Biol Chem 273(50):33311-9 |




