Glutathione transferases in bacteria

Allocati, Nerino; Federici, L.; Masulli, Michele; Ilio, Carmine Di

doi:10.1111/j.1742-4658.2008.06743.x

Cited by 309 publications

(282 citation statements)

References 152 publications

(299 reference statements)

Supporting

Mentioning

274

Contrasting

Unclassified

Order By: Relevance

“…Although Gst Pm -4 possesses no cysteine, it is able to conjugate the model substrates CDNB and GSH, which means it belongs to the GST superfamily [30,31]. Considering the fact that it is generally accepted that proteins with >40% sequence identity belong to the same class, Gst Pm -4 resembling a new branch GST (IsoJ) from Rhodococcus AD45 was confirmed that it belonged to a new class of GST [2].…”

Section: Discussionmentioning

confidence: 96%

“…The glutathione S-transferases (GSTs; EC 2.5.1.18) are a family of multifunctional proteins that can facilitate the nucleophilic attack of GSH to a large variety of reactive electrophilic endobiotic and xenobiotic [1,2]. GSTs are widely distributed in natural organisms and are found in both eukaryotes and prokaryotes.…”

Section: Introductionmentioning

confidence: 99%

“…Now, bacterial GSTs are also referred as part of a superfamily of enzymes that play a key role in cellular detoxification processes. Besides its role in detoxification, bacterial GSTs are also involved in a variety of distinct metabolic pathways such as the biotransformation of dichloromethane, the degradation of lignin and atrazine, and the reductive dechlorination of pentachlorophenol [2].…”

Section: Introductionmentioning

confidence: 99%

“…Bacterial GSTs are mainly referred as four different classes: beta, chi, theta and zeta [1,2,4,6,7]. Beta class of cytoplasmic GSTs (cGSTs), characterized by the presence of a cysteine residue at the GSH site, is able to conjugate the model substrate 1-chloro-2,4-dinitrobenzene (CDNB) and bind to the GSH-affinity matrix [6].…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

A glutathione S-transferase from Proteus mirabilis involved in heavy metal resistance and its potential application in removal of Hg2+

Zhang

Yin

et al. 2013

Journal of Hazardous Materials

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A glutathione S-transferase from Proteus mirabilis involved in heavy metal resistance and its potential application in removal of Hg2+

Zhang

Yin

et al. 2013

Journal of Hazardous Materials

View full text Add to dashboard Cite

“…For example, GST participates in protecting cells against the damage of oxidative stress (43,44), and Ysr29 repression of GST levels may prevent an aberrant response to this stress. In addition, OmpA is an outer membrane protein known to play a role in the pathogenesis of E. coli K1 and acts as an adhesin, invasin, and immune evasin (45)(46)(47).…”

Section: Discussionmentioning

confidence: 99%

Global discovery of small RNAs in Yersinia pseudotuberculosis identifies Yersinia -specific small, noncoding RNAs required for virulence

Koo¹,

Alleyne

Schiano³

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

101

175

View full text Add to dashboard Cite

A major class of bacterial small, noncoding RNAs (sRNAs) acts by base-pairing with mRNAs to alter the translation from and/or stability of the transcript. Our laboratory has shown that Hfq, the chaperone that mediates the interaction of many sRNAs with their targets, is required for the virulence of the enteropathogen Yersinia pseudotuberculosis. This finding suggests that sRNAs play a critical role in the regulation of virulence in this pathogen, but these sRNAs are not known. Using a deep sequencing approach, we identified the global set of sRNAs expressed in vitro by Y. pseudotuberculosis. Sequencing of RNA libraries from bacteria grown at 26°C and 37°C resulted in the identification of 150 unannotated sRNAs. The majority of these sRNAs are Yersinia specific, without orthologs in either Escherichia coli or Salmonella typhimurium. Six sRNAs are Y. pseudotuberculosis specific and are absent from the genome of the closely related species Yersinia pestis. We found that the expression of many sRNAs conserved between Y. pseudotuberculosis and Y. pestis differs in both timing and dependence on Hfq, suggesting evolutionary changes in posttranscriptional regulation between these species. Deletion of multiple sRNAs in Y. pseudotuberculosis leads to attenuation of the pathogen in a mouse model of yersiniosis, as does the inactivation in Y. pestis of a conserved, Yersinia-specific sRNA in a mouse model of pneumonic plague. Finally, we determined the regulon controlled by one of these sRNAs, revealing potential virulence determinants in Y. pseudotuberculosis that are regulated in a posttranscriptional manner.Ysr29 | RybB | stress | Illumina-Solexa | 2D-DIGE

show abstract

Dechlorination of polychlorobiphenyl degradation metabolites by a recombinant glutathione S‐transferase from Acidovorax sp. KKS102

Shehu

Alias

2019

FEBS Open Bio

View full text Add to dashboard Cite

A glutathione S ‐transferase ( GST ) with a potential dehalogenation function against various organochlorine substrates was identified from a polychlorobiphenyl ( PCB )‐degrading organism, Acidovorax sp. KKS 102. A homolog of the gene BphK (biphenyl upper pathway K), named BphK‐ KKS , was cloned, purified and biochemically characterized. Bioinformatic analysis indicated several conserved amino acids that participated in the catalytic activity of the enzyme, and site‐directed mutagenesis of these conserved amino acids revealed their importance in the enzyme's catalytic activity. The wild‐type and mutant (C10F, K107T and A180P) recombinant proteins displayed wider substrate specificity. The wild‐type recombinant GST reacted towards 1‐chloro‐2,4‐dinitrobenzene ( CDNB ), ethacrynic acid, hydrogen peroxide and cumene hydroperoxide. The mutated recombinant proteins, however, showed significant variation in specific activities towards the substrates. A combination of a molecular docking study and a chloride ion detection assay showed potential interaction with and a dechlorination function against 2‐, 3‐ and 4‐chlorobenzoates (metabolites generated during PCB biodegradation) in addition to some organochlorine pesticides (dichlorodiphenyltrichloroethane, endosulfan and permethrin). It was demonstrated that the behavior of the dechlorinating activities varied among the wild‐type and mutant recombinant proteins. Kinetic studies (using CDNB and glutathione) showed that the kinetic parameters K m , V max , K cat and K m / K cat were all affected by the mutations. While C10F and A180P mutants displayed an increase in GST activity and the dechlorination function of the enzyme, the K107T mutant displayed variable results, suggesting a functional role of Lys107 in determining substrate specificity of the enzyme. These results demonstrated that the enzyme should be valuable in the bioremediation of metabolites generated during PCB biodegradation.

show abstract

Glutathione transferases in bacteria

Cited by 309 publications

References 152 publications

A glutathione S-transferase from Proteus mirabilis involved in heavy metal resistance and its potential application in removal of Hg2+

A glutathione S-transferase from Proteus mirabilis involved in heavy metal resistance and its potential application in removal of Hg2+

Global discovery of small RNAs in Yersinia pseudotuberculosis identifies Yersinia -specific small, noncoding RNAs required for virulence

Dechlorination of polychlorobiphenyl degradation metabolites by a recombinant glutathione S‐transferase from Acidovorax sp. KKS102

Contact Info

Product

Resources

About