scholarly journals Structures of yeast glutathione‐ S ‐transferase Gtt2 reveal a new catalytic type of GST family

EMBO Reports ◽  
2009 ◽  
Vol 10 (12) ◽  
pp. 1320-1326 ◽  
Author(s):  
Xiao‐Xiao Ma ◽  
Yong‐Liang Jiang ◽  
Yong‐Xing He ◽  
Rui Bao ◽  
Yuxing Chen ◽  
...  
Keyword(s):  
Glutathione S Transferase ◽  
Gst Family

scholarly journals Molecular Evolution of the Glutathione S-Transferase Family in the Bemisia tabaci Species Complex

2020 ◽  
Vol 12 (2) ◽  
pp. 3857-3872 ◽  
Author(s):  
Ofer Aidlin Harari ◽  
Diego Santos-Garcia ◽  
Mirit Musseri ◽  
Pnina Moshitzky ◽  
Mitulkumar Patel ◽  
...  
Keyword(s):  
Molecular Evolution ◽  
Bemisia Tabaci ◽  
Tertiary Structure ◽  
Synonymous Substitution ◽  
Diet Breadth ◽  
Glutathione S Transferase ◽  
New Host ◽  
Delta Sigma ◽  
Environmentally Responsive ◽  
Gst Family

Abstract The glutathione S-transferase (GST) family plays an important role in the adaptation of herbivorous insects to new host plants and other environmental constrains. The family codes for enzymes that neutralize reactive oxygen species and phytotoxins through the conjugation of reduced glutathione. Here, we studied the molecular evolution of the GST family in Bemisia tabaci, a complex of >35 sibling species, differing in their geographic and host ranges. We tested if some enzymes evolved different functionality, by comparing their sequences in six species, representing five of the six major genetic clades in the complex. Comparisons of the nonsynonymous to synonymous substitution ratios detected positive selection events in 11 codons of 5 cytosolic GSTs. Ten of them are located in the periphery of the GST dimer, suggesting a putative involvement in interactions with other proteins. Modeling the tertiary structure of orthologous enzymes, identified additional 19 mutations in 9 GSTs, likely affecting the enzymes’ functionality. Most of the mutation events were found in the environmentally responsive classes Delta and Sigma, indicating a slightly different delta/sigma tool box in each species. At a broader genomic perspective, our analyses indicated a significant expansion of the Delta GST class in B. tabaci and a general association between the diet breadth of hemipteran species and their total number of GST genes. We raise the possibility that at least some of the identified changes improve the fitness of the B. tabaci species carrying them, leading to their better adaptation to specific environments.

Glutathione S-transferase (GST) family in barley: Identification of members, enzyme activity, and gene expression pattern

2013 ◽  
Vol 170 (14) ◽  
pp. 1277-1284 ◽  
Author(s):  
Mohammad Kazem Rezaei ◽  
Zahra-Sadat Shobbar ◽  
Maryam Shahbazi ◽  
Raha Abedini ◽  
Sajjad Zare
Keyword(s):  
Gene Expression ◽  
Enzyme Activity ◽  
Expression Pattern ◽  
Gene Expression Pattern ◽  
Glutathione S Transferase ◽  
Gst Family

scholarly journals Structure of the complete dimeric human GDAP1 core domain provides insights into ligand binding and clustering of disease mutations

2020 ◽  
Author(s):  
Giang Thi Tuyet Nguyen ◽  
Aleksi Sutinen ◽  
Arne Raasakka ◽  
Gopinath Muruganandam ◽  
Remy Loris ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Glutathione S Transferase ◽  
Oligomeric State ◽  
Core Domain ◽  
Charcot Marie Tooth Disease ◽  
Disease Mutations ◽  
And Function ◽  
Allosteric Mechanisms ◽  
Gst Family ◽  
Tooth Disease

ABSTRACTCharcot-Marie-Tooth disease (CMT) is one of the most common inherited neurological disorders. Despite the common involvement of ganglioside-induced differentiation-associated protein 1 (GDAP1) in CMT, the protein structure and function, as well as the pathogenic mechanisms, remain unclear. We determined the crystal structure of the complete human GDAP1 core domain, which shows a novel mode of dimerization within the glutathione S-transferase (GST) family. The long GDAP1-specific insertion forms an extended helix and a flexible loop. GDAP1 is catalytically inactive towards classical GST substrates. Through metabolite screening, we identified a ligand for GDAP1, the fatty acid hexadecanedioic acid, which is relevant for mitochondrial membrane permeability and Ca2+ homeostasis. The fatty acid binds to a pocket next to a CMT-linked residue cluster, increases protein stability, and induces changes in protein conformation and oligomerization. The closest homologue of GDAP1, GDAP1L1, is monomeric in its full-length form. Our results highlight the uniqueness of GDAP1 within the GST family and point towards allosteric mechanisms in regulating GDAP1 oligomeric state and function.

scholarly journals Genome-wide identification and expression analysis of the glutathione S-transferase (GST) family under different developmental tissues and abiotic stresses in Chinese cabbage (Brassica rapa ssp. pekinensis)

2018 ◽  
Author(s):  
Jiangtao Du ◽  
Jie Ren ◽  
Xueling Ye ◽  
Ailin Hou ◽  
Wei Fu ◽  
...  
Keyword(s):  
Brassica Rapa ◽  
Chinese Cabbage ◽  
Abiotic Stresses ◽  
Environmental Changes ◽  
Cadmium Stress ◽  
Stress Conditions ◽  
Glutathione S Transferase ◽  
Genome Wide ◽  
High And Low Temperatures ◽  
Gst Family

The glutathione-S-transferase (GST) family of proteins is ancient and versatile, and plays an important role in combating exogenous pathogens, endogenous toxicants, and various abiotic stresses. Although the GST family has been studied in many crops, few studies have been reported in Chinese cabbage (Brassica rapa ssp. Pekinensis). In the present work, genome-wide analysis of the GST family in Chinese cabbage was carried out, and the expression and functions of genes under different conditions were investigated. A total of 88 GST genes were identified and divided into seven subfamilies according to their evolutionary relationships. Tandem duplication of genes was revealed as the main mechanism of expansion in this family. Transcriptome analysis under high and low temperatures and abiotic stress conditions revealed that most GST genes respond to environmental changes to varying degrees, particularly under herbicide and cadmium stress conditions. Our findings provide a basis for analysing the functions of GST family members in Chinese cabbage, especially in response to various abiotic stresses.

Influence of GSTM1, GSTT1, and GSTP1 genetic polymorphisms on disorders in transplant patients: a systematic review

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Murilo Pita-Oliveira ◽  
Fernanda Rodrigues-Soares
Keyword(s):  
Oxidative Stress ◽  
Systematic Review ◽  
Glutathione S Transferase ◽  
Transplant Patients ◽  
Enzymatic Function ◽  
Therapeutic Outcomes ◽  
Pubmed Database ◽  
Genes Encoding ◽  
Repair Ability ◽  
Gst Family

Abstract The glutathione-S-transferase (GST) enzymes are phase II isoenzymes responsible for protection against free radicals and xenobiotics. Since these proteins are described as polymorphic, polymorphisms in genes that encode them may alter enzymatic function and contribute to oxidative stress. In this context, such polymorphisms were already associated with several diseases and multiple therapeutic outcomes. A systematic review was performed to evaluate studies regarding the association between polymorphisms in three genes encoding enzymes of the GST family – GSTM1, GSTT1, and GSTP1 – and disorders in transplant patients. A total of 125 articles on which inclusion and exclusion criteria were applied were identified at PubMed database. Thirty-two studies met the target criteria and were included in the review. The mechanisms by which GST genotypes influence the development of disorders in transplant patients differ by disorder: they may participate in it by decreasing metabolism of drugs administered to patients undergoing transplantation, then exposing them to greater toxicity; by decreasing the repair ability against oxidative stress; or by encoding proteins that may be recognized as foreign, setting of an alloimmune reaction. Although some results are better established – such as GSTM1 null genotype’s role in the development of toxicity events in transplant patients – others require further evidences, as GST influence on the development of pulmonary decline and posttransplant diabetes mellitus (PTDM). The importance of investigating these associations lies in a personalized medicine, in which the high-risk genotype patient has its treatment individualized and its care for prophylaxis and surveillance increased, potentially reducing this population’s morbimortality.

Relationship between glutathione S-transferase M1, T1, and P1 polymorphisms and chronic lymphocytic leukemia

Blood ◽  
2002 ◽  
Vol 99 (11) ◽  
pp. 4216-4218 ◽  
Author(s):  
Martin Yuille ◽  
Alison Condie ◽  
Chantelle Hudson ◽  
Zsofia Kote-Jarai ◽  
Elaine Stone ◽  
...  
Keyword(s):  
High Risk ◽  
Chronic Lymphocytic Leukemia ◽  
Hematologic Malignancies ◽  
Lymphocytic Leukemia ◽  
Polymorphic Variation ◽  
Glutathione S Transferase ◽  
Risk Alleles ◽  
Glutathione S Transferases ◽  
Increasing Risk ◽  
Gst Family

Interindividual differences in susceptibility to hematologic malignancies may be mediated in part through polymorphic variability in the bioactivation and detoxification of carcinogens. The glutathione S–transferases (GSTs) have been implicated as susceptibility genes in this context for a number of cancers. The aim of this study was to examine whether polymorphic variation in GSTs confers susceptibility to chronic lymphocytic leukemia (CLL). GSTM1, GSTT1, andGSTP1 genotypes were determined in 138 patients and 280 healthy individuals. The frequency of both GSTM1 andGSTT1 null genotypes and the GSTP1-Ile allele was higher in cases than in controls. There was evidence of a trend in increasing risk with the number of putative “high-risk” alleles of the GST family carried (P = .04). The risk of CLL associated with possession of all 3 “high-risk” genotypes was increased 2.8-fold (OR = 2.8, 95% confidence interval: 1.1-6.9). Our findings suggest that heritable GST status may influence the risk of developing CLL.

scholarly journals Glutathione S-Transferases in Marine Copepods

2021 ◽  
Vol 9 (9) ◽  
pp. 1025
Author(s):  
Chiara Lauritano ◽  
Ylenia Carotenuto ◽  
Vittoria Roncalli
Keyword(s):  
Cellular Localization ◽  
Detoxification Enzymes ◽  
Reduced Form ◽  
Glutathione S Transferase ◽  
Status Monitoring ◽  
Wide Range ◽  
Glutathione S Transferases ◽  
Gst Family ◽  
Marine Copepods

The glutathione S-transferase (GST) is a complex family of phase II detoxification enzymes, known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to a wide variety of endogenous and exogenous electrophilic compounds for detoxification purposes. In marine environments, copepods are constantly exposed to multiple exogenous stressors, thus their capability of detoxification is key for survival. Full identification of the GST family in copepods has been limited only to few species. As for insects, the GST family includes a wide range of genes that, based on their cellular localization, can be divided in three classes: cytosolic, microsomal, and mitochondrial. The role of GSTs might have class-specific features, thus understanding the nature of the GST family has become crucial. This paper covers information of the GST activity in marine copepods based on studies investigating gene expression, protein content, and enzymatic activity. Using published literature and mining new publicly available transcriptomes, we characterized the multiplicity of the GST family in copepods from different orders and families, highlighting the possible role of these genes as biomarker for ocean health status monitoring.

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