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NTH1  -  alpha,alpha-trehalase NTH1

Saccharomyces cerevisiae S288c

Synonyms: Alpha,alpha-trehalase, Alpha,alpha-trehalose glucohydrolase, NTH, Neutral trehalase, YD8119.07C, ...
 
 
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Disease relevance of NTH1

  • However, heat stress induces an increase in NTH1 mRNA in the tpk1tpk2TPK3 mutant [1].
  • No significant acceleration was observed in the repair of either a single AP site cleaved by the bifunctional glycosylase NTH of E. coli or the repair of a single 8-oxoguanine, initiated by the bifunctional glycosylase OGG1 [2].
  • Deletion of nth1 confirmed that Nth1p is responsible for the majority of activity for thymine glycol and AP site incision in the absence of metal ions, while nth1 mutants exhibit hypersensitivity to methylmethanesulfonate (MMS) [3].
 

High impact information on NTH1

  • We therefore propose that the NTH1 and NTH2 genes have stress-related function and the gene products may be called stress proteins [4].
  • The neutral trehalase is responsible for intracellular hydrolysis of trehalose, in contrast to the acid trehalase, which is responsible for utilization of extracellular trehalose [4].
  • Experiments with a mutant disrupted in the YBR0106 ORF showed, in contrast to a NTH1 deletion mutant, no changes in trehalase activity and in trehalose concentration [5].
  • Resequencing of the neutral trehalase gene NTH1 on chromosome IV resulted in the observation of two possible start codons (Kopp, M., Nwaka, S., and Holzer, H. (1994) Gene (Amst.) 150, 403-404) [5].
  • However, similar to the NTH1 gene a requirement of the intact YBR0106 gene for thermotolerance is demonstrated in experiments with the respective mutants [5].
 

Biological context of NTH1

 

Anatomical context of NTH1

 

Associations of NTH1 with chemical compounds

 

Regulatory relationships of NTH1

 

Other interactions of NTH1

 

Analytical, diagnostic and therapeutic context of NTH1

References

  1. Stability of neutral trehalase during heat stress in Saccharomyces cerevisiae is dependent on the activity of the catalytic subunits of cAMP-dependent protein kinase, Tpk1 and Tpk2. Zähringer, H., Holzer, H., Nwaka, S. Eur. J. Biochem. (1998) [Pubmed]
  2. Effect of S. cerevisiae APN1 protein on mammalian DNA base excision repair. Bogliolo, M., Cappelli, E., D'Osualdo, A., Rossi, O., Barbieri, O., Kelley, M.R., Frosina, G. Anticancer Res. (2003) [Pubmed]
  3. Roles of base excision repair enzymes Nth1p and Apn2p from Schizosaccharomyces pombe in processing alkylation and oxidative DNA damage. Sugimoto, T., Igawa, E., Tanihigashi, H., Matsubara, M., Ide, H., Ikeda, S. DNA Repair (Amst.) (2005) [Pubmed]
  4. Molecular biology of trehalose and the trehalases in the yeast Saccharomyces cerevisiae. Nwaka, S., Holzer, H. Prog. Nucleic Acid Res. Mol. Biol. (1998) [Pubmed]
  5. Expression and function of the trehalase genes NTH1 and YBR0106 in Saccharomyces cerevisiae. Nwaka, S., Kopp, M., Holzer, H. J. Biol. Chem. (1995) [Pubmed]
  6. Induction of neutral trehalase Nth1 by heat and osmotic stress is controlled by STRE elements and Msn2/Msn4 transcription factors: variations of PKA effect during stress and growth. Zähringer, H., Thevelein, J.M., Nwaka, S. Mol. Microbiol. (2000) [Pubmed]
  7. Response to oxidative stress caused by H(2)O(2) in Saccharomyces cerevisiae mutants deficient in trehalase genes. Pedreño, Y., Gimeno-Alcañiz, J.V., Matallana, E., Argüelles, J.C. Arch. Microbiol. (2002) [Pubmed]
  8. Deletion of the ATH1 gene in Saccharomyces cerevisiae prevents growth on trehalose. Nwaka, S., Mechler, B., Holzer, H. FEBS Lett. (1996) [Pubmed]
  9. Purification and characterization of neutral trehalase from the yeast ABYS1 mutant. App, H., Holzer, H. J. Biol. Chem. (1989) [Pubmed]
  10. Neutral trehalase Nth1p of Saccharomyces cerevisiae encoded by the NTH1 gene is a multiple stress responsive protein. Zähringer, H., Burgert, M., Holzer, H., Nwaka, S. FEBS Lett. (1997) [Pubmed]
  11. Molecular cloning, characterisation, and expression of a neutral trehalase from the insect pathogenic fungus Metarhizium anisopliae. Xia, Y., Gao, M., Clarkson, J., Charnley, A. J. Invertebr. Pathol. (2002) [Pubmed]
  12. Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae. Kopp, M., Müller, H., Holzer, H. J. Biol. Chem. (1993) [Pubmed]
  13. Two distinct pathways for trehalose assimilation in the yeast Saccharomyces cerevisiae. Jules, M., Guillou, V., François, J., Parrou, J.L. Appl. Environ. Microbiol. (2004) [Pubmed]
  14. Evidence for contribution of neutral trehalase in barotolerance of Saccharomyces cerevisiae. Iwahashi, H., Nwaka, S., Obuchi, K. Appl. Environ. Microbiol. (2000) [Pubmed]
  15. Substrate specificity of the phosphorylated fructose-1,6-bisphosphatase dephosphorylating protein phosphatase from Saccharomyces cerevisiae. Manhart, A., Holzer, H. Yeast (1988) [Pubmed]
  16. A role for calcium in the regulation of neutral trehalase activity in the fission yeast Schizosaccharomyces pombe. Franco, A., Soto, T., Vicente-Soler, J., Paredes, V., Madrid, M., Gacto, M., Cansado, J. Biochem. J. (2003) [Pubmed]
  17. Molecular cloning of the neutral trehalase gene from Kluyveromyces lactis and the distinction between neutral and acid trehalases. Amaral, F.C., Van Dijck, P., Nicoli, J.R., Thevelein, J.M. Arch. Microbiol. (1997) [Pubmed]
 
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