Disease relevance of GstD6

• The amino acid sequence identity of class-Theta subunits is highly conserved in rat, the fruitfly Drosophila, maize (Zea mays) and Methylobacterium, which suggests that this family is representative of the ancient progenitor GST gene and originates from the endosymbioses of a purple bacterium leading to the mitochondrion [1].
• Each housefly GST cDNA was inserted into a bacterial plasmid expression system and a glutathione transferase activity was expressed in Escherichia coli [2].

High impact information on GstD6

• We propose that the Drosophila gst D genes provide a unique system for studying GST gene regulation, in vivo physiological functions, and evolution of substrate specificities with a global perspective [3].
• Two of the genes are probably GST pseudogenes in that their open reading frames are shorter than functional GSTs, and no RNAs from them have been detected thus far [3].
• The patterns of sequence similarity in pairwise comparisons of the family members suggest that gene conversion may have played a role in the evolution of this GST multigene family [3].
• We find that within the PTM region, the cysteine residues required for GST-type activity are unnecessary for invertebrate CLIC function, but that specific residues within the proposed transmembrane helix are necessary for correct targeting and protein function [4].
• We report the cDNA sequence for rat glutathione transferase (GST) subunit 5, which is one of at least three class Theta subunits in this species [1].

Biological context of GstD6

• This mini review describes the insect GST enzyme family, focusing specifically on their role in conferring insecticide resistance [5].
• These molecules could be considered as members of the GST superfamily, where the T cruzi protein may take a particular place because of its internal gene duplication [6].
• Members of these two GST classes are clustered on chromosome arms 2L and 3R respectively [7].
• The sequences of individual oligonucleotides included the following consensus sequences; 5'-ACCA-3', 5'-ACCCA-3', 5'-CTATCA-3' and 5'-TGCC-3'. The oligonucleotides including these consensus sequences were show to have significant affinity with the GST-RAE28 fusion protein [8].
• Pull-down experiments using glutathione beads/GST-fusion proteins indicate a direct interaction of LG4 with syndecan-4, which might be the major receptor for cell adhesion [9].

Anatomical context of GstD6

• By creating GST (glutathione S-transferase)-fused LG1, LG2, LG4 and LG5 proteins, we found that only LG4 is active for the adhesion of human HT1080 cells, human umbilical vein endothelial cells and Drosophila haemocytes Kc167 with a half-saturating concentration of 20 microg/ml [9].

Associations of GstD6 with chemical compounds

• The other pathway depends on the presence of glutathione (GSH) and glutathione transferase (GST) [10].
• This sequence, when compared with that of subunit 12 recently published by Ogura, Nishiyama, Okada, Kajita, Narihata, Watabe, Hiratsuka & Watabe [(1991) Biochem. Biophys. Res. Commun. 181, 1294-1300] proves that Theta is a separate multigene class of GST with little amino acid sequence identity with Mu-, Alpha- or Pi-class enzymes [1].
• Eleven CYP genes and three glutathione S-transferases (GST) genes were significantly induced by phenobarbital, seven CYP and one GST gene were induced by atrazine [11].

Analytical, diagnostic and therapeutic context of GstD6

• Indeed, mammalian two-hybrid assays, GST fusion protein pull-down assays, and co-immunoprecipitation assays showed that Sp1ZFDBD and Sp1ID are able to interact with corepressor proteins such as SMRT, NcoR, and BCoR [12].
• This molecular interaction was confirmed by GST-fusion protein pull-down assays and by co-immunoprecipitation experiments [13].

References