High impact information on GUT2

• Studies on the functionally isolated enzymes demonstrated that neither Nde1p nor Nde2p directly inhibits Gut2p [1].
• Subsequently, glycerol 3-phosphate donates electrons to the respiratory chain via mitochondrial glycerol-3-phosphate dehydrogenase (Gut2p) [1].
• Second, the activation of NADH dehydrogenase inhibited the Gut2p in such a manner that, at a saturating concentration of NADH, glycerol 3-phosphate is not used as respiratory substrate [2].
• Mass spectrometric analysis of a tryptic digest of the corresponding 2D-gel spot identified the protein as the GUT2 gene product, the FAD-dependent mitochondrial glycerol-3-phosphate dehydrogenase [3].
• This was confirmed by the lack of specific labeling in mitochondria from a gut2 deletion strain [3].

Biological context of GUT2

• Derepression of GUT2 requires the protein kinase Snflp as well as the heteromeric protein complex, Hap2/3/4/5, and its putative DNA-binding site (UASHAP) located in the promoter region [4].
• The Saccharomyces cerevisiae glycerol-3-phosphate dehydrogenase (GUT2) promoter and part of the protein-coding region have been isolated on a 6.3-kb genomic DNA fragment [5].
• Both Nde1p/Nde2p and Gut2p are located in the inner mitochondrial membrane with catalytic sites facing the intermembranal space [2].
• The cloned gene has been mapped both physically and genetically to the left arm of chromosome IX, where the original gut2 mutation also maps [6].
• The nucleotide sequence of a 3.2 kb PstI-XhoI fragment complementing a gut2 mutant strain is presented [6].

Associations of GUT2 with chemical compounds

• Transcriptional analysis of the GUT2 gene showed that it was repressed by glucose and derepressed on the non-fermentable carbon sources, glycerol, lactate and ethanol [4].
• Carbon source-dependent transcriptional regulation of the mitochondrial glycerol-3-phosphate dehydrogenase gene, GUT2, from Saccharomyces cerevisiae [4].
• Furthermore, glucose repression of GUT2 requires the negative regulator, Opi1p [4].

Other interactions of GUT2

• In that mutant, transcript levels from GUT1 and GUT2 are highly attenuated compared with those of the wild-type parent when both are grown on glycerol-based medium [7].
• NDE1 and NDE2 encode isoenzymes of mitochondrial external NADH dehydrogenase; GUT2 encodes a key enzyme of the glycerol-3-phosphate shuttle [8].
• DAR1 is distinct from GUT2, which encodes a glucose-repressed mitochondrial G3PDase, but is identical to GPD1 from S. cerevisiae, a close relative of S. diastaticus [9].
• In addition, we have identified Gut2, the mitochondrial FAD-dependent glycerol-3-phosphate dehydrogenase, as a new substrate for Imp1 [10].

References