High impact information on GCV2

• This protein protected a 17-base pair CATCN7CTTCTT region of GCV2 that is conserved between GCV1 and GCV2 [1].
• In an heterologous CYC1 promoter the region needed for the glycine response of GCV2 (encoding the P-subunit of glycine decarboxylase) mediated repression that was relieved by glycine [1].
• A reporter plasmid containing a DNA sequence from the GCV2 promoter which confers glycine regulation on heterologous genes was introduced into the yeast deletion set to screen for genes required for glycine regulation [2].
• Deletion analysis of the GCV2 promoter delimited the control region which contains putative regulatory sites for GCN4 and GLN3 transcription factors [3].
• Expression of GCV2 was induced by the addition of more than 200 microM glycine in the medium, and a maximal sixfold induction occurred above 1 mM [3].

Biological context of GCV2

• A protein was identified that bound to the glycine regulatory regions of GCV1 and GCV2 only if the CTTCTT motif was intact [1].
• Furthermore, deletion analyses and mutagenesis have shown that the palindromic sequence is important for full repression of GCV2 in complex glucose-containing medium and functions in a manner that is different from control mediated by the GATA element [4].

Associations of GCV2 with chemical compounds

• In yeast, lipoamide dehydrogenase functions in at least three multienzyme complexes: pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase (which function in the entry of pyruvate into, and metabolism via, the citric acid cycle) and glycine decarboxylase [5].
• A new mutation introducing a one-carbon requirement (e.g., formate) for the glycine-supplemented growth of a serine-glycine auxotroph (ser1) was correlated with a lack of glycine decarboxylase activity [6].
• L-protein is the dihydrolipoamide dehydrogenase component of the glycine decarboxylase complex which catalyses, with serine hydroxymethyltransferase, the mitochondrial step of photorespiration [7].
• Lipoic acid is a coenzyme that is essential for the activity of enzyme complexes such as those of pyruvate dehydrogenase and glycine decarboxylase [8].

References