GUT2/YIL155C Summary Help

Standard Name GUT2 1
Systematic Name YIL155C
Feature Type ORF, Verified
Description Mitochondrial glycerol-3-phosphate dehydrogenase; expression is repressed by both glucose and cAMP and derepressed by non-fermentable carbon sources in a Snf1p, Rsf1p, Hap2/3/4/5 complex dependent manner (2, 3, 4, 5 and see Summary Paragraph)
Name Description Glycerol UTilization 6
Chromosomal Location
ChrIX:53708 to 51759 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All GUT2 GO evidence and references
  View Computational GO annotations for GUT2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 11 genes
Classical genetics
Large-scale survey
37 total interaction(s) for 34 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 5
  • Co-fractionation: 1
  • Co-purification: 1

Genetic Interactions
  • Negative Genetic: 8
  • Phenotypic Enhancement: 5
  • Phenotypic Suppression: 5
  • Positive Genetic: 8
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 1
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 649
Molecular Weight (Da) 72,388
Isoelectric Point (pI) 7.9
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIX:53708 to 51759 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 1994-12-10 | Sequence: 1994-12-10
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1950 53708..51759 1994-12-10 1994-12-10
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 SGDIDS000001417

Under aerobic conditions, S. cerevisiae are able to utilize glycerol as a sole carbon and energy source. Glycerol degradation, shown here, is a two-step process mediated by the gene products of GUT1 and GUT2. GUT1 encodes a glycerol kinase that converts glycerol to glycerol-3-phosphate in the cytosol. The product of this reaction is transported to the mitochondria where it is oxidized to dihydroxyacetone by the membrane protein Gut2p, a glycerol-3-phosphate dehydrogenase. Dihydroxyacetone is then transported back to the cytosol where it enters into either glycolysis or gluconeogenesis (7, 8, 6).

In addition to glycerol degradation, Gut2p also participates in the glycerol-3-phosphate shuttle, which is required for S. cerevisiae to maintain redox balance between NAD and NADH under aerobic conditions. Gut2p is involved in oxidizing excess cytoplasmic NADH in the mitochondria as part of a complex that includes the NADH dehydrogenases Nde1p and Nde2p, and the lactate dehydrogenases Dld1p and Cyb2p (9). Gut2p activity is inhibited by ATP/ADP as well as NADH dehydrogenase activation (10, 4).

GUT2 gene expression is carbon source regulated; transcription is repressed when cells are grown on fermentable carbon sources such as glucose and induced on non-fermentable carbon sources such as glycerol or ethanol (7, 11, 3). On non-fermentable carbon sources, GUT2 induction requires the protein kinase Snf1p and the transcription-activating Hap2p/Hap3p/Hap4p/Hap5p complex (3). Conversely, the negative regulator Opi1p facilitates GUT2 repression (11, 3). Mutations in the human homolog of GUT2, GPD2 (OMIM; 12), have been associated with the noninsulin-dependent form of diabetes mellitus (type II; OMIM; 13).

Last updated: 2006-02-17 Contact SGD

References cited on this page View Complete Literature Guide for GUT2
1) Ronnow, B. and Kielland-Brandt, M.C.  (1992) Personal Communication, Mortimer Map Edition 11
2) Tadi D, et al.  (1999) Selection of genes repressed by cAMP that are induced by nutritional limitation in Saccharomyces cerevisiae. Yeast 15(16):1733-45
3) Grauslund M and Ronnow B  (2000) Carbon source-dependent transcriptional regulation of the mitochondrial glycerol-3-phosphate dehydrogenase gene, GUT2, from Saccharomyces cerevisiae. Can J Microbiol 46(12):1096-100
4) Pahlman IL, et al.  (2002) Kinetic regulation of the mitochondrial glycerol-3-phosphate dehydrogenase by the external NADH dehydrogenase in Saccharomyces cerevisiae. J Biol Chem 277(31):27991-5
5) Lu L, et al.  (2003) Rsf1p, a protein required for respiratory growth of Saccharomyces cerevisiae. Curr Genet 43(4):263-72
6) Ronnow B and Kielland-Brandt MC  (1993) GUT2, a gene for mitochondrial glycerol 3-phosphate dehydrogenase of Saccharomyces cerevisiae. Yeast 9(10):1121-30
7) Sprague GF and Cronan JE  (1977) Isolation and characterization of Saccharomyces cerevisiae mutants defective in glycerol catabolism. J Bacteriol 129(3):1335-42
8) Pavlik P, et al.  (1993) The glycerol kinase (GUT1) gene of Saccharomyces cerevisiae: cloning and characterization. Curr Genet 24(1-2):21-5
9) Grandier-Vazeille X, et al.  (2001) Yeast mitochondrial dehydrogenases are associated in a supramolecular complex. Biochemistry 40(33):9758-69
10) Albertyn J, et al.  (1992) Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae. FEBS Lett 308(2):130-2
11) Grauslund M, et al.  (1999) Expression of GUT1, which encodes glycerol kinase in Saccharomyces cerevisiae, is controlled by the positive regulators Adr1p, Ino2p and Ino4p and the negative regulator Opi1p in a carbon source-dependent fashion. Nucleic Acids Res 27(22):4391-8
12) Brown LJ, et al.  (1996) Structural organization and mapping of the human mitochondrial glycerol phosphate dehydrogenase-encoding gene and pseudogene. Gene 172(2):309-12
13) Novials A, et al.  (1997) Mutation in the calcium-binding domain of the mitochondrial glycerophosphate dehydrogenase gene in a family of diabetic subjects. Biochem Biophys Res Commun 231(3):570-2