Immunogold localization of glutathione transferase B1‐1 in <i>Proteus mirabilis</i>

Allocati, Nerino; Cellini, Luigina; Aceto, Antonio; Iezzi, T; Angelucci, Stefania; Robuffo, Iole; Ilio, Carmine Di

doi:10.1016/0014-5793(94)01115-x

Cited by 12 publications

(13 citation statements)

References 21 publications

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“…Studies on the interaction of PmGST B1-1 with a number of antimicrobial agents indicated that this enzyme was able to sequester antibiotics with avidity [14,16]. Indeed, our previous studies demonstrated the presence of PmGST B1-1 not only in the cytoplasm but also in the periplasmic compartment [37]. In addition, structural data indicate that there is a hydrophobic cavity large enough to bind an antibiotic molecule located at the dimer interface of the enzyme [18].…”

Section: Discussionmentioning

confidence: 95%

Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses

Allocati

Favaloro

Masulli

et al. 2003

Biochemical Journal

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We investigated the effects of several xenobiotics, including antimicrobial agents and general stress factors such as starvation, heat and osmotic shock, on the modulation of expression of Proteus mirabilis glutathione S-transferase B1-1 (PmGST B1-1). The level of expression of PmGST B1-1 was established by both Western- and Northern-blot experiments. Our results show that several compounds can modulate expression of PmGST B1-1. The level of PmGST B1-1 increased when bacterial cells were exposed to a variety of stresses such as 1-chloro-2,4-dinitrobenzene, H(2)O(2), fosfomycin or tetracycline. A knock-out gst B gene was also constructed using the suicide vector pKNOCKlox-Ap. Successful inactivation of the wild-type gene was confirmed by PCR, DNA sequence analysis and Western blotting. Under normal culture conditions, this mutant was viable and displayed no significant phenotypic differences compared with the wild-type. However, viability tests revealed that the null mutant was more sensitive to oxidative stress in the form of H(2)O(2) and to several antimicrobial drugs when compared with the wild-type. These results suggest that PmGST B1-1 has an active role in the protection against oxidative stress generated by H(2)O(2) and it appears to be involved in the detoxification of antimicrobial agents.

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Section: Discussionmentioning

confidence: 95%

Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses

Allocati

Favaloro

Masulli

et al. 2003

Biochemical Journal

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“…On the contrary, a high degree of specific labelling was detected for the bacteria grown in the presence of toxic 4-chlorophenol concentrations ( Fig. A predominant localisation of a GST species had already been observed in Proteus mirabilis [30]. Moreover, as shown in Fig.…”

Section: Localisation Of Gst and Msramentioning

confidence: 89%

Expression of glutathioneS-transferase and peptide methionine sulphoxide reductase inOchrobactrum anthropiis correlated to the production of reactive oxygen species caused by aromatic substrates

Tamburro¹,

Robuffo²,

Heipieper³

et al. 2004

FEMS Microbiology Letters

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Peptide methionine sulphoxide reductase (MsrA) and glutathione S-transferases (GSTs) are considered as detoxification enzymes. In the xenobiotics-degrading bacterium Ochrobactrum anthropi the two enzymes are co-induced by toxic concentrations of aromatic substrates such as phenol and 4-chlorophenol. In aerobic organisms, degradation of aromatic substrates by mono- and dioxygenases leads to a generation of oxidative stress that causes the occurrence of reactive oxygen species (ROS). A capillary electrophoretic method, using the intracellular conversion of dihydrorhodamine-123 into rhodamine-123, was developed to measure the content of ROS in the bacteria. The presence of toxic concentrations of the aromatic substrate 4-chlorophenol, an inducer of GST and MsrA, leads to a significant increase in the production of ROS. These results strongly suggest that GST and MsrA enzymes are part of the bacterial defence mechanism against particular oxidative stress conditions. As oxidative stress is known to be present predominantly close to the cytoplasmic membrane, we investigated the subcellular distribution of both MsrA and GST enzymes in this bacterium grown in the presence of 4-chlorophenol. By Western blotting, MsrA and GST was assayed in the cytoplasm as well as in the periplasm. Moreover, immunolocalisation by colloidal gold immunoelectron microscopy identified the two proteins associated with the cell envelope.

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“…Finally, crystallographic data highlighted the presence of a hydrophobic cavity large enough to bind antibacterial molecules located at the dimer interface [12]. These results were strengthened by the preponderant periplasmic location of the enzyme in the periplasmic space [81].…”

Section: Functionsmentioning

confidence: 99%

Glutathione transferases in bacteria

et al. 2008

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Bacterial glutathione transferases (GSTs) are part of a superfamily of enzymes that play a key role in cellular detoxification. GSTs are widely distributed in prokaryotes and are grouped into several classes. Bacterial GSTs are implicated in a variety of distinct processes such as the biodegradation of xenobiotics, protection against chemical and oxidative stresses and antimicrobial drug resistance. In addition to their role in detoxification, bacterial GSTs are also involved in a variety of distinct metabolic processes such as the biotransformation of dichloromethane, the degradation of lignin and atrazine, and the reductive dechlorination of pentachlorophenol. This review article summarizes the current status of knowledge regarding the functional and structural properties of bacterial GSTs.

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Immunogold localization of glutathione transferase B1‐1 in Proteus mirabilis

Cited by 12 publications

References 21 publications

Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses

Proteus mirabilis glutathione S-transferase B1-1 is involved in protective mechanisms against oxidative and chemical stresses

Expression of glutathioneS-transferase and peptide methionine sulphoxide reductase inOchrobactrum anthropiis correlated to the production of reactive oxygen species caused by aromatic substrates

Glutathione transferases in bacteria

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