NTH1/YDR001C Summary Help

Standard Name NTH1 1
Systematic Name YDR001C
Feature Type ORF, Verified
Description Neutral trehalase, degrades trehalose; required for thermotolerance and may mediate resistance to other cellular stresses; may be phosphorylated by Cdc28p; inhibited by Dcs1p; NTH1 has a paralog, NTH2, that arose from the whole genome duplication (1, 2, 3, 4, 5, 6 and see Summary Paragraph)
Name Description Neutral TreHalase 1
Chromosomal Location
ChrIV:452475 to 450220 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All NTH1 GO evidence and references
  View Computational GO annotations for NTH1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Regulators 8 genes
Classical genetics
Large-scale survey
97 total interaction(s) for 56 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 23
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 6
  • Biochemical Activity: 9
  • Co-purification: 1
  • Reconstituted Complex: 5
  • Two-hybrid: 4

Genetic Interactions
  • Dosage Rescue: 2
  • Negative Genetic: 27
  • Phenotypic Enhancement: 9
  • Positive Genetic: 7
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 1
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 751
Molecular Weight (Da) 85,879
Isoelectric Point (pI) 7.82
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:452475 to 450220 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2256 452475..450220 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002408

Trehalose is a storage carbohydrate that can either be synthesized by the cell or obtained from the external environment, and is converted by trehalase with water into two glucose molecules (7). S. cerevisiae has two trehalase enzymes, an acid trehalase encoded by ATH1 (8) and a neutral trehalase encoded by NTH1 (1). A third locus, NTH2, is 77% identical to NTH1, but does not appear to encode a trehalase activity, or be involved in trehalose catabolism, since an nth2 null mutant exhibits normal levels of neutral trehalase activity and trehalose (3).

NTH1 is induced by various stresses including exposure to heat, hydrogen peroxide, or cycloheximide (2). Nth1p is a cytoplasmic homodimer required for the hydrolysis of intracellular trehalose (1), and is involved in thermotolerance through a mechanism that does not appear to correspond to trehalose abundance (3). Phosphorylation by Cdc28p has been predicted to activate Nth1p. Deletion of NTH1 results in complete loss of neutral trehalase activity, accumulation of internal trehalose, and heat sensitivity.

Last updated: 2005-08-12 Contact SGD

References cited on this page View Complete Literature Guide for NTH1
1) Kopp M, et al.  (1993) Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae. J Biol Chem 268(7):4766-74
2) Zahringer H, et al.  (1997) Neutral trehalase Nth1p of Saccharomyces cerevisiae encoded by the NTH1 gene is a multiple stress responsive protein. FEBS Lett 412(3):615-20
3) Nwaka S, et al.  (1995) Expression and function of the trehalase genes NTH1 and YBR0106 in Saccharomyces cerevisiae. J Biol Chem 270(17):10193-8
4) Ubersax JA, et al.  (2003) Targets of the cyclin-dependent kinase Cdk1. Nature 425(6960):859-64
5) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
6) Schepers W, et al.  (2012) In Vivo Phosphorylation of Ser21 and Ser83 during Nutrient-induced Activation of the Yeast Protein Kinase A (PKA) Target Trehalase. J Biol Chem 287(53):44130-42
7) Francois J and Parrou JL  (2001) Reserve carbohydrates metabolism in the yeast Saccharomyces cerevisiae. FEMS Microbiol Rev 25(1):125-45
8) Alizadeh P and Klionsky DJ  (1996) Purification and biochemical characterization of the ATH1 gene product, vacuolar acid trehalase, from Saccharomyces cerevisiae. FEBS Lett 391(3):273-8