Stress induction of the <i>Bacillus subtilis clpP</i> gene encoding a homologue of the proteolytic component of the Clp protease and the involvement of ClpP and ClpX in stress tolerance

Gerth, Ulf; Krüger, Elke; Derré, Isabelle; Msadek, Tarek; Hecker, Michael

doi:10.1046/j.1365-2958.1998.00840.x

Cited by 186 publications

(173 citation statements)

References 78 publications

(126 reference statements)

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“…In this work, we identified the clpP gene of S. agalactiae and showed that its product, the serine protease ClpP, is involved in the regulation of growth at high temperatures and survival under stress conditions, including heat shock, as already shown in the case of B. subtilis (Gerth et al, 1998), L. monocytogenes (Gaillot et al, 2000) and S. pneumoniae (Chastanet et al, 2001). Consistently, in all these bacteria, the synthesis of ClpP is induced under stress conditions including heat shock (Chastanet et al, 2001;Derre et al, 1999;Gaillot et al, 2001).…”

Section: Discussionsupporting

confidence: 69%

“…Defects in cell division as a result of mutations in the clp genes have also been observed in B. subtilis and L. monocytogenes, suggesting that proteins involved in cell morphology or cell division are controlled either directly or indirectly by the ClpXP protease complexes (Gerth et al, 1998;Nair et al, 1999). In C. crescentus, ClpXP is required in vivo for the cell-cycle-dependent degradation of the regulatory protein CtrA (Jenal & Fuchs, 1998).…”

Section: Discussionmentioning

confidence: 99%

“…The ClpP proteins of various prokaryotes, including B. subtilis (Gerth et al, 1998) and the facultative intracellular pathogen L. monocytogenes (Gaillot et al, 2000), have been shown to play an essential role in stress tolerance. To determine the role of ClpP in GBS stress tolerance, we constructed an S. agalactiae strain lacking a functional ClpP (DclpP) and an S. agalactiae DclpP complemented strain (DclpPc) (see Methods).…”

Section: Clpp Is Required For Growth Under Different Stress Conditionsmentioning

confidence: 99%

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Role of the Streptococcus agalactiae ClpP serine protease in heat-induced stress defence and growth arrest

et al. 2003

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The main causes of microbial death after heat exposure are not well understood. Here, it is shown that the heat-shock protein ClpP plays a major role in heat-induced growth arrest in Streptococcus agalactiae. A mutant lacking the ClpP protease was more sensitive to the inhibitory effects of heat, salt and oxidative stress than the isogenic wild-type strain. During growth arrest, this mutant displayed important modifications of its total protein content, including a decreased level of essential metabolic enzymes such as the alcohol dehydrogenase. Analysis of protein carbonylation demonstrated that the ClpP protease plays a role in preventing accelerated protein oxidation. Higher levels of oxidized DnaK, a key modulator of the heat-shock regulon, were observed in the ClpP mutant and these were increased following heat shock. Accumulation of oxidized/inactivated DnaK might explain why the ClpP mutant was unable to properly synthesize DNA and proteins, and why it exhibited an aberrant cell morphology. Even though ClpP plays a minor role in the virulence of S. agalactiae in a murine infection model, the data presented here point to the importance of ClpP in oxidative stress defence in preventing heat-induced cell alterations.

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Section: Discussionsupporting

confidence: 69%

Section: Discussionmentioning

confidence: 99%

Section: Clpp Is Required For Growth Under Different Stress Conditionsmentioning

confidence: 99%

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Role of the Streptococcus agalactiae ClpP serine protease in heat-induced stress defence and growth arrest

et al. 2003

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“…The Clp proteases consist of two multimeric components, an ATPase and a proteolytic component, both of which are required for proteolysis (6). In B. subtilis, three Clp ATPases (ClpC, ClpE, and ClpX) and one proteolytic component (ClpP) have been described (2,4,5,21). Therefore, knockouts of all four clp genes and the ftsH gene were tested to determine whether they conferred stability to the tagged HrcA variants.…”

Section: Vol 183 2001mentioning

confidence: 99%

SsrA-Mediated Tagging in Bacillus subtilis

2001

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A general mechanism in bacteria to rescue stalled ribosomes involves a stable RNA encoded by the ssrA gene. This RNA, termed tmRNA, encodes a proteolytic peptide tag which is cotranslationally added to truncated polypeptides, thereby targeting them for rapid proteolysis. To study this ssrA-mediated mechanism in Bacillus subtilis, a bipartite detection system was constructed that was composed of the HrcA transcriptional repressor and the bgaB reporter gene coding for a heat-stable ␤-galactosidase fused to an HrcA-controlled promoter. After the predicted proteolysis tag was fused to HrcA, the reporter ␤-galactosidase was expressed constitutively at a high level due to the instability of the tagged HrcA. Replacement of the two C-terminal alanine residues of the tag by aspartate rendered the repressor stable. Replacement of the hrcA stop codon by a transcriptional terminator sequence rendered the protein unstable; this was caused by trans translational addition of the proteolytic tag. Inactivating the B. subtilis ssrA or smpB (yvaI) gene prevented the trans translational tagging reaction. Various protease-deficient strains of B. subtilis were tested for proteolysis of tagged HrcA. HrcA remained stable only in clpX or clpP knockouts, which suggests that this ATP-dependent protease is primarily responsible for the degradation of SsrA-tagged proteins in B. subtilis.What happens to translating ribosomes arriving at the 3Ј end of an mRNA molecule lacking a stop codon? Will they fall off (dissociate) or remain stalled? Work carried out over the last 5 years with Escherichia coli has shown that the ribosomes first are stalled and then are released by a novel mechanism designated trans translation (for a recent review, see reference 13). This mechanism requires a small stable RNA (SsrA RNA), also termed 10Sa RNA or tmRNA, which serves both as a tRNA and as an mRNA. When translating ribosomes arrive at the 3Ј end of a truncated mRNA without encountering a stop codon, the process of trans translation is initiated. A tmRNA charged with alanine at its 3Ј end (17, 28) enters the acceptor position of the ribosome and this is followed by transfer of the alanine residue to the nascent polypeptide chain.

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“…De multiples protéines Clp ont ainsi été identifiées et classées en deux sous-familles : les protéases, notamment ClpP [17] et les Clp-ATPases, chaperons moléculaires présentant aussi une activité ATPasique [21]. La protéase ClpP est une Hsp jouant un rôle clef tant lors d'un stress qu'au cours de la croissance [7,9]. L'activité protéolytique de ClpP est modulée par son association avec des protéines de la sous-famille des Clp-ATPases.…”

Section: Introductionunclassified

Article

Beltramo¹,

Grandvalet²,

Guzzo³

2003

Lait

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-Expression of Oenococcus oeni clpP-clpL locus in response to environmental conditions. The Oenococcus oeni lactic acid bacterium, mainly responsible for malolactic fermentation during winemaking processes, is confronted with various stresses including the presence of ethanol or low pH. The tolerance of this bacterium to stress is essential for its growth in wine. Comprehension of mechanisms involved in stress response is required for the control of malolactic starters. One of these mechanisms is based on the synthesis of stress proteins. This study deals with clp genes, which were known to play a central role in stress response and also in microbial development. The genome of O. oeni contains two genes surprisingly located in the same locus, encoding ClpP and ClpL proteins. The aim of this work was to characterize the clpP-clpL locus and the transcriptional expression during growth and following stress. In order to quantify the transcript ratios, a quantitative real-time reverse transcription-PCR experiment was set up. Finally, the regulation mechanisms of the O. oeni stress genes were discussed.Lactic acid bacteria / Oenococcus oeni / stress response / clp gene / transcription Résumé -La bactérie lactique Oenococcus oeni, souvent responsable de la fermentation malolactique lors du processus de vinification, est confrontée à de multiples stress, tels que la présence d'éthanol ou un pH faible. La tolérance de cette bactérie vis-à-vis de ces stress est essentielle à sa croissance dans un milieu vin donc la maîtrise des levains malolactiques nécessite l'étude et la compréhension des mécanismes impliqués dans la réponse au stress. L'un de ces mécanismes repose sur la production de protéines de stress et parmi ces dernières, la famille des protéines Clp joue un rôle majeur tant lors de stress qu'au cours de la croissance. Le gène clpP a été identifié chez O. oeni I.O.B. 8413. Il faut remarquer l'organisation génétique atypique de ce locus. En effet, chez O. oeni, le gène situé en aval de clpP code une protéine similaire à une Clp-ATPase de la classe ClpL. L'objectif de ce travail a été de caractériser le locus clpP-clpL et d'étudier son expression au niveau transcriptionnel suite à un stress et au cours de la croissance. Afin de pouvoir quantifier de façon relative l'expression des gènes de stress, la technique de PCR quantitative en temps réel a été mise en oeuvre. Enfin, des mécanismes potentiels de régulation des gènes de stress chez O. oeni sont proposés.Bactérie lactique / Oenococcus oeni / réponse au stress / gène clp / transcription * Auteur correspondant : jean.guzzo@u-bourgogne.fr 88 C. Beltramo et al.

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Stress induction of the Bacillus subtilis clpP gene encoding a homologue of the proteolytic component of the Clp protease and the involvement of ClpP and ClpX in stress tolerance

Cited by 186 publications

References 78 publications

Role of the Streptococcus agalactiae ClpP serine protease in heat-induced stress defence and growth arrest

Role of the Streptococcus agalactiae ClpP serine protease in heat-induced stress defence and growth arrest

SsrA-Mediated Tagging in Bacillus subtilis

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