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TDH3  -  glyceraldehyde-3-phosphate dehydrogenase...

Saccharomyces cerevisiae S288c

Synonyms: G7576, GAPDH 3, GLD1, GPD3, Glyceraldehyde-3-phosphate dehydrogenase 3, ...
 
 
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Disease relevance of TDH3

  • We describe the construction and analysis of derivatives of the yeast TDH3 promoter in which the TATA box element has been replaced by a portion of the phage lambda operator containing a consensus TATA site flanked by binding sites for the cI repressor [1].
  • Although both alternatives lead to impaired survival under starvation conditions, only constitutively autophagic strains, carrying a multicopy plasmid with the csc1-1 allele under the control of the TDH3 promoter, undergo accelerated autolysis in the experimental conditions tested [2].
 

High impact information on TDH3

 

Biological context of TDH3

  • The levels of activation by these deletions of transcription mediated through either the segment of TDH3 promoter or the segment of ADH1 (alcohol dehydrogenase 1 gene) promoter were quantitatively examined and the region between -583 and -447 was found to be required for full transcriptional activation with either promoter segment [7].
  • The promoter region of the TDH3 gene is known to exhibit high transcriptional activity regardless of the fermentability of the carbon source and has been widely utilized to synthesize heterologous gene products in S. cerevisiae [8].
  • These data demonstrate that the presence of a functional TDH2 or TDH3 allele is required for cell growth [9].
  • The potentiation of the GRF1 UAS by this element occurs when placed upstream from the TATA box of either the TDH3 or CYC1 promoters [10].
  • A synthetic DNA element comprising this sequence, or an analogue in which two of the degenerate nucleotides of the GRF1 site consensus sequence were altered, activated 5' deleted TDH3 and CYC1 promoters [10].
 

Anatomical context of TDH3

 

Associations of TDH3 with chemical compounds

  • The upstream activating sequence (UAS) of TDH3, one of three genes encoding glyceraldehyde phosphate dehydrogenase in Saccharomyces cerevisiae, was characterized by using a series of external and internal deletion mutants of the TDH3 upstream region [7].
  • Mutant strains lacking only a functional TDH2 allele or a TDH3 allele grow at 50 and 75% of the rate observed for wild type cells, respectively, when glucose is used as carbon source [9].
  • Using a 2D-gel system to study protein carbonylation, it is shown in this work that both Tdh2p and Tdh3p isozymes were oxidized during exposure to H(2)O(2) [13].
  • When the deleted version of the neo sequence retaining only one additional ATG (NeoD) was expressed under the control of a TDH3 promoter whose UAS was deleted, the transformed cells were unable to grow at a low concentration of the antibiotic G418 [14].
  • The self-cloning TDH3p-ATF1 yeast strain produced a higher amount of isoamyl acetate [15].
 

Regulatory relationships of TDH3

  • Surprisingly, the UAS fragment composed of the 22-mer sequence containing exclusively a RAP1 binding sequence showed full activation, suggesting that the RAP1-dependent transcriptional activation is a primary positive control in the TDH3 gene expression [7].
  • In a mutant which lacks the trans-activating protein GCR1 and which as a consequence expresses TDH3 at less than 5% of the wild-type level, the chromatin structure is different [16].
 

Other interactions of TDH3

  • These findings suggest that ABF1 functions as a glucose-dependent transactivator for the expression of the TDH3 gene [17].
  • The TDH3 structural gene encodes two resolvable forms of glyceraldehyde-3-phosphate dehydrogenase which differ by their net charge [18].
  • Site-specific deletion and promoter reconstruction experiments suggest that the entire activation potential of the -676 to -381 region of the TDH3 gene promoter may be accounted for by a combination of the GRF1 site and the GPE [10].
  • To investigate whether h-AP can indeed replace the S. cerevisiae phosphoglycerate kinase, a multi-copy plasmid carrying the h-AP gene under control of the yeast TDH3 promoter was introduced into a pgk1 delta mutant of S. cerevisiae [19].
  • In order to determine whether this requirement reflects the need for heat-shock protein (hsp), we analysed the effect of heat shock on rp-mRNA levels in several yeast strains in which each of the heat-shock genes encoding hsp26, hsp35 or hsp83 had been individually disrupted [20].
 

Analytical, diagnostic and therapeutic context of TDH3

  • Using the yeast three-hybrid screen and RNA gel shift analysis, we have found that the protein GLD-1, a germline-specific protein and a member of the STAR family of RNA-binding proteins, specifically binds to the TGEs [3].

References

  1. A temperature-sensitive lambda cI repressor functions on a modified operator in yeast cells by masking the TATA element. Wedler, H., Wambutt, R. Mol. Gen. Genet. (1995) [Pubmed]
  2. Overexpression of csc1-1. A plausible strategy to obtain wine yeast strains undergoing accelerated autolysis. Cebollero, E., Martinez-Rodriguez, A., Carrascosa, A.V., Gonzalez, R. FEMS Microbiol. Lett. (2005) [Pubmed]
  3. The STAR protein, GLD-1, is a translational regulator of sexual identity in Caenorhabditis elegans. Jan, E., Motzny, C.K., Graves, L.E., Goodwin, E.B. EMBO J. (1999) [Pubmed]
  4. The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum. Esnault, Y., Blondel, M.O., Deshaies, R.J., Scheckman, R., Képès, F. EMBO J. (1993) [Pubmed]
  5. Differential protein S-thiolation of glyceraldehyde-3-phosphate dehydrogenase isoenzymes influences sensitivity to oxidative stress. Grant, C.M., Quinn, K.A., Dawes, I.W. Mol. Cell. Biol. (1999) [Pubmed]
  6. Self-association of the single-KH-domain family members Sam68, GRP33, GLD-1, and Qk1: role of the KH domain. Chen, T., Damaj, B.B., Herrera, C., Lasko, P., Richard, S. Mol. Cell. Biol. (1997) [Pubmed]
  7. The UAS of the yeast GAPDH promoter consists of multiple general functional elements including RAP1 and GRF2 binding sites. Yagi, S., Yagi, K., Fukuoka, J., Suzuki, M. J. Vet. Med. Sci. (1994) [Pubmed]
  8. Fermentable and nonfermentable carbon sources sustain constitutive levels of expression of yeast triosephosphate dehydrogenase 3 gene from distinct promoter elements. Kuroda, S., Otaka, S., Fujisawa, Y. J. Biol. Chem. (1994) [Pubmed]
  9. Isolation and characterization of yeast strains carrying mutations in the glyceraldehyde-3-phosphate dehydrogenase genes. McAlister, L., Holland, M.J. J. Biol. Chem. (1985) [Pubmed]
  10. A multi-component upstream activation sequence of the Saccharomyces cerevisiae glyceraldehyde-3-phosphate dehydrogenase gene promoter. Bitter, G.A., Chang, K.K., Egan, K.M. Mol. Gen. Genet. (1991) [Pubmed]
  11. The glyceraldehyde-3-phosphate dehydrogenase polypeptides encoded by the Saccharomyces cerevisiae TDH1, TDH2 and TDH3 genes are also cell wall proteins. Delgado, M.L., O'Connor, J.E., Azorín, I., Renau-Piqueras, J., Gil, M.L., Gozalbo, D. Microbiology (Reading, Engl.) (2001) [Pubmed]
  12. Candida albicans TDH3 gene promotes secretion of internal invertase when expressed in Saccharomyces cerevisiae as a glyceraldehyde-3-phosphate dehydrogenase-invertase fusion protein. Delgado, M.L., Gil, M.L., Gozalbo, D. Yeast (2003) [Pubmed]
  13. Hydrogen peroxide-induced carbonylation of key metabolic enzymes in Saccharomyces cerevisiae: the involvement of the oxidative stress response regulators Yap1 and Skn7. Costa, V.M., Amorim, M.A., Quintanilha, A., Moradas-Ferreira, P. Free Radic. Biol. Med. (2002) [Pubmed]
  14. Expression enhancement of the Tn5 neomycin-resistance gene by removal of upstream ATG sequences and its use for probing heterologous upstream activating sequences in yeast. Yagi, S., Yagi-Tanaka, K., Yoshioka, J., Suzuki, M. Curr. Genet. (1993) [Pubmed]
  15. Construction of a self-cloning sake yeast that overexpresses alcohol acetyltransferase gene by a two-step gene replacement protocol. Hirosawa, I., Aritomi, K., Hoshida, H., Kashiwagi, S., Nishizawa, Y., Akada, R. Appl. Microbiol. Biotechnol. (2004) [Pubmed]
  16. The chromatin structure at the promoter of a glyceraldehyde phosphate dehydrogenase gene from Saccharomyces cerevisiae reflects its functional state. Pavlović, B., Hörz, W. Mol. Cell. Biol. (1988) [Pubmed]
  17. The glucose-dependent transactivation activity of ABF1 on the expression of the TDH3 gene in yeast. Jung, S.Y., Yoo, H.Y., Kim, Y.H., Kim, J., Rho, H.M. Curr. Genet. (1995) [Pubmed]
  18. Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes. McAlister, L., Holland, M.J. J. Biol. Chem. (1985) [Pubmed]
  19. Human acylphosphatase cannot replace phosphoglycerate kinase in Saccharomyces cerevisiae. Van Hoek, P., Modesti, A., Ramponi, G., Kötter, P., van Dijken, J.P., Pron, J.T. Antonie Van Leeuwenhoek (2001) [Pubmed]
  20. Known heat-shock proteins are not responsible for stress-induced rapid degradation of ribosomal protein mRNAs in yeast. Galego, L., Barahona, I., Alves, A.P., Vreken, P., Raué, H.A., Planta, R.J., Rodrigues-Pousada, C. Yeast (1993) [Pubmed]
 
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