Anti-stress activity of Propionibacterium freudenreichii: identification of a reactivative protein

Vorobjeva, Lena I.; Leverrier, Pauline; Zinchenko, Anatoly; Boyaval, Patrick; Khodjaev, E.Yu.; Varioukhina, Svetlana Yu.; Ponomareva, G. M.; Гордеева, Е. А.; Jan, Gwénaël

doi:10.1023/b:anto.0000020276.18127.99

Cited by 16 publications

(10 citation statements)

References 46 publications

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“…Our study represents the first report strongly suggesting CS as a key player in plant response to Al-stress. In P. freudenreichii, CS was also induced by the detergents and heat [57]. In A. thaliana, CS cytosolic gene Atcys-3 A is transcriptionally upregulated by Cd 21 exposure, bringing about an increase in GSH synthesis [37], supporting our present result (Fig.…”

supporting

confidence: 90%

Identification of aluminum‐responsive proteins in rice roots by a proteomic approach: Cysteine synthase as a key player in Al response

et al. 2007

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Aluminum (Al) toxicity is a serious limitation to worldwide crop production. Rice is one of the most Al-tolerant crops and also serves as an important monocot model plant. This study aims to identify Al-responsive proteins in rice, based on evidence that Al resistance is an inducible process. Two Al treatment systems were applied in the study: Al 31 -containing simple Ca solution culture and Al 31-containing complete nutrient solution culture. Proteins prepared from rice roots were separated by 2-DE. The 2-DE patterns were compared and the differentially expressed proteins were identified by MS. A total of 17 Al-responsive proteins were identified, with 12 of those being up-regulated and 5 down-regulated. Among the up-regulated proteins are copper/ zinc superoxide dismutase (Cu-Zn SOD), GST, and S-adenosylmethionine synthetase 2, which are the consistently known Al-induced enzymes previously detected at the transcriptional level in other plants. More importantly, a number of other identified proteins including cysteine synthase (CS), 1-aminocyclopropane-1-carboxylate oxidase, G protein b subunit-like protein, abscisic acid-and stress-induced protein, putative Avr9/Cf-9 rapidly elicited protein 141, and a 33 kDa secretory protein are novel Al-induced proteins. Most of these proteins are functionally associated with signaling transduction, antioxidation, and detoxification. CS, as consistently detected in both Al stress systems, was further validated by Western blot and CS activity assays. Moreover, the metabolic products of CS catalysis, i.e. both the total glutathione pool and reduced glutathione, were also significantly increased in response to Al stress. Taken together, our results suggest that antioxidation and detoxification ultimately related to sulfur metabolism, particularly to CS, may play a functional role in Al adaptation for rice.

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confidence: 90%

Identification of aluminum‐responsive proteins in rice roots by a proteomic approach: Cysteine synthase as a key player in Al response

et al. 2007

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“…2003). Extracellular proteins that confer a protective effect have also been reported for E. coli and Propionibacterium freudenreichii (Vorobjeva et al. 2004; Nikolaev 2006).…”

Section: Discussionmentioning

confidence: 84%

Extracellular protectants produced byClostridium perfringenscells at elevated temperatures

Heredia

Ybarra

García-Hernández

et al. 2009

Letters in Applied Microbiology

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Aim: The mechanisms of adaptation of Clostridium perfringens to high temperatures are not well understood. In this work, the involvement of extracellular compounds in protection to heat was determined. Methods and Results: Cells were grown in fluid thioglycollate medium or chicken broth. When mid‐log phase was reached, they were heat‐shocked at 50°C for 30 min. Then cultures were centrifuged and supernatants were transferred to nonshocked cells. Heat tolerance of these cells was performed at 55°C. Viable cells were determined. In some cases, supernatants were heated at 65°C or 100°C or treated with trypsin. Supernatants were fractionated and PAGE was made of fractions showing heat‐protective activity. When C. perfringens was exposed to a heat shock at 50°C, extracellular factors were found in the culture supernatant that provided protection to cells not exposed to a heat shock. The extracellular factors were sensitive to heat and trypsin treatment suggesting a protein component. SDS‐PAGE analysis of supernatant fractions from heat‐treated cells revealed two induced proteins (56 and 125 kDa) that could be involved in heat tolerance. Conclusion: In this work, the presence and thermoprotective activity of extracellular factors produced by C. perfringens under a heat shock was demonstrated. Significance and Impact of the Study: The detection of thermoprotective extracellular factors of C. perfringens will aid in our understanding of the physiology of survival of C. perfringens in foods.

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“…Expression of cysK has been reported to be a general response to stress in bacteria and plants (5,57,71,73). In bacteria, cysteine is synthesized from O-acetylserine and H 2 S catalyzed by O-acetylserine sulfhydrolase (CysK) while O-acetylserine is produced from serine and acetyl-CoA catalyzed by serine acetyltransferase (CysE) (12,29).…”

Section: Discussionmentioning

confidence: 99%

Cytochrome bd Oxidase, Oxidative Stress, and Dioxygen Tolerance of the Strictly Anaerobic Bacterium Moorella thermoacetica

Das¹,

Silaghi-Dumitrescu

Ljungdahl³

et al. 2005

J Bacteriol

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The gram-positive, thermophilic, acetogenic bacterium Moorella thermoacetica can reduce CO 2 to acetate via the Wood-Ljungdahl (acetyl coenzyme A synthesis) pathway. This report demonstrates that, despite its classification as a strict anaerobe, M. thermoacetica contains a membrane-bound cytochrome bd oxidase that can catalyze reduction of low levels of dioxygen. Whole-cell suspensions of M. thermoacetica had significant endogenous O 2 uptake activity, and this activity was increased in the presence of methanol or CO, which are substrates in the Wood-Ljungdahl pathway. Cyanide and azide strongly (ϳ70%) inhibited both the endogenous and CO/methanol-dependent O 2 uptake. UV-visible light absorption and electron paramagnetic resonance spectra of n-dodecyl-␤-maltoside extracts of M. thermoacetica membranes showed the presence of a cytochrome bd oxidase complex containing cytochrome b 561 , cytochrome b 595 , and cytochrome d (chlorin). Subunits I and II of the bd oxidase were identified by N-terminal amino acid sequencing. The M. thermoacetica cytochrome bd oxidase exhibited cyanide-sensitive quinol oxidase activity. The M. thermoacetica cytochrome bd (cyd) operon consists of four genes, encoding subunits I and II along with two ABC-type transporter proteins, homologs of which in other bacteria are required for assembly of the bd complex. The level of this cyd operon transcript was significantly increased when M. thermoacetica was grown in the absence of added reducing agent (cysteine ؉ H 2 S). Expression of a 35-kDa cytosolic protein, identified as a cysteine synthase (CysK), was also induced by the nonreducing growth conditions. The combined evidence indicates that cytochrome bd oxidase and cysteine synthase protect against oxidative stress and contribute to the limited dioxygen tolerance of M. thermoacetica.Dioxygen is the preferred electron sink in the respiratory chain of most aerobic bacteria (58). Cytochrome oxidases are the membrane-bound, terminal components of the dioxygendependent respiratory chain, which reduces dioxygen to water with formation of pH and potential gradients (6, 45). Two main types of respiratory cytochrome oxidases are known in bacteria: the heme/copper oxidases (cytochrome aa 3 , cytochrome caa 3 oxidase, and cytochrome bo oxidase), and the heme-only cytochrome bd quinol oxidase, which is associated with microaerobic dioxygen respiration (24,56,59,62). Cytochrome bd oxidases purified from aerobic bacteria have been characterized as 1:1 heterodimers of two integral membrane proteins referred to as subunits I and II (35,55). The heterodimers contain three heme components: a low-spin heme, b 558 , and two high-spin hemes, b 595 and d. In the genomes of Escherichia coli (31) and Azotobacter vinelandii (41), subunits I and II are encoded by cydA and cydB, respectively, of the cytochrome bd (cyd) operon. Two ABC-type transporter proteins, CydD and CydC, are typically required for assembly of the cytochrome bd complex in both gram-positive and gram-negative aerobic bacteria (14, 60). Aerobic r...

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Anti-stress activity of Propionibacterium freudenreichii: identification of a reactivative protein

Cited by 16 publications

References 46 publications

Identification of aluminum‐responsive proteins in rice roots by a proteomic approach: Cysteine synthase as a key player in Al response

Identification of aluminum‐responsive proteins in rice roots by a proteomic approach: Cysteine synthase as a key player in Al response

Extracellular protectants produced byClostridium perfringenscells at elevated temperatures

Cytochrome bd Oxidase, Oxidative Stress, and Dioxygen Tolerance of the Strictly Anaerobic Bacterium Moorella thermoacetica

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