ClpL Is Required for Folding of CtsR in Streptococcus mutans

Tao, Liang; Biswas, Indranil

doi:10.1128/jb.01743-12

Cited by 28 publications

(41 citation statements)

References 55 publications

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“…Under stress conditions, GroEL is titrated away from HrcA by accumulating denatured proteins, which drives the equilibrium toward aggregated/inactive HrcA (321) (298). A recent report provided evidence that S. mutans ClpL interacts with CtsR both in vivo and in vitro and, by its chaperone activity, prevents CtsR from aggregating under ambient growth conditions (323).…”

Section: Treating Damaged Macromoleculesmentioning

confidence: 99%

Stress Physiology of Lactic Acid Bacteria

Papadimitriou

Alegría

Bron

et al. 2016

Microbiol Mol Biol Rev

521

404

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SUMMARYLactic acid bacteria (LAB) are important starter, commensal, or pathogenic microorganisms. The stress physiology of LAB has been studied in depth for over 2 decades, fueled mostly by the technological implications of LAB robustness in the food industry. Survival of probiotic LAB in the host and the potential relatedness of LAB virulence to their stress resilience have intensified interest in the field. Thus, a wealth of information concerning stress responses exists today for strains as diverse as starter (e.g.,Lactococcus lactis), probiotic (e.g., severalLactobacillusspp.), and pathogenic (e.g.,EnterococcusandStreptococcusspp.) LAB. Here we present the state of the art for LAB stress behavior. We describe the multitude of stresses that LAB are confronted with, and we present the experimental context used to study the stress responses of LAB, focusing on adaptation, habituation, and cross-protection as well as on self-induced multistress resistance in stationary phase, biofilms, and dormancy. We also consider stress responses at the population and single-cell levels. Subsequently, we concentrate on the stress defense mechanisms that have been reported to date, grouping them according to their direct participation in preserving cell energy, defending macromolecules, and protecting the cell envelope. Stress-induced responses of probiotic LAB and commensal/pathogenic LAB are highlighted separately due to the complexity of the peculiar multistress conditions to which these bacteria are subjected in their hosts. Induction of prophages under environmental stresses is then discussed. Finally, we present systems-based strategies to characterize the “stressome” of LAB and to engineer new food-related and probiotic LAB with improved stress tolerance.

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Section: Treating Damaged Macromoleculesmentioning

confidence: 99%

Stress Physiology of Lactic Acid Bacteria

Papadimitriou

Alegría

Bron

et al. 2016

Microbiol Mol Biol Rev

521

404

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“…For acid induction, 5 ml of culture was harvested, washed with saline, and resuspended in 5 ml of THY broth at pH 5.5 for 2 h, a signal pH that has been demonstrated to induce acid adaptation of S. mutans effectively (11); cells grown at pH 7.0 were used as a control. GusA activity was measured as described earlier (34). General stress response.…”

Section: Methodsmentioning

confidence: 99%

SMU.746-SMU.747, a Putative Membrane Permease Complex, Is Involved in Aciduricity, Acidogenesis, and Biofilm Formation in Streptococcus mutans

Król

Biswas

King

et al. 2013

Journal of Bacteriology

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Dental caries induced by Streptococcus mutans is one of the most prevalent chronic infectious diseases worldwide. The pathogenicity of S. mutans relies on the bacterium's ability to colonize tooth surfaces and survive a strongly acidic environment. We performed an ISS1 transposon mutagenesis to screen for acid-sensitive mutants of S. mutans and identified an SMU.746-SMU.747 gene cluster that is needed for aciduricity. SMU.746 and SMU.747 appear to be organized in an operon and encode a putative membrane-associated permease. SMU.746-and SMU.747-deficient mutants showed a reduced ability to grow in acidified medium. However, the short-term or long-term acid survival capacity and F 1 F 0 ATPase activity remained unaffected in the mutants. Furthermore, deletion of both genes did not change cell membrane permeability and the oxidative and heat stress responses. Growth was severely affected even with slight acidification of the defined medium (pH 6.5). The ability of the mutant strain to acidify the defined medium during growth in the presence of glucose and sucrose was significantly reduced, although the glycolysis rate was only slightly affected. Surprisingly, deletion of the SMU.746-SMU.747 genes triggered increased biofilm formation in low-pH medium. The observed effects were more striking in a chemically defined medium. We speculate that the SMU.746-SMU.747 complex is responsible for amino acid transport, and we discuss its possible role in colonization and survival in the oral environment.

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“…We therefore wanted to study whether ClpC or ClpE could also recognize SsbA protein for degradation. For this, we introduced the plasmid carrying SsbA with the N-terminal histidine (His) tag into the IBSJ2 (Δ clpC ) and IBSJ5 (Δ clpE ) strains (25). Expression of the SsbA protein was then evaluated in these strains at the mid-logarithmic-growth phase by Western blotting.…”

Section: Resultsmentioning

confidence: 99%

Strain-Dependent Recognition of a Unique Degradation Motif by ClpXP in Streptococcus mutans

Jana

Tao

Biswas

2016

mSphere

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Regulated proteolysis in bacteria is an important biological process that maintains protein homeostasis. ClpXP, an intracellular proteolytic complex, is the primary protease that is responsible for protein turnover. While the substrates for ClpXP were identified in Escherichia coli, the substrates for vast majority of bacteria are currently unknown. In this study, we identified a unique substrate for ClpXP-mediated degradation in Streptococcus mutans, a dental pathogen. We also found that a small motif composed of 3 amino acids is sufficient for ClpXP-mediated degradation. Identification of this motif will clearly help us to understand the pathogenesis of this organism and other related pathogens.

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ClpL Is Required for Folding of CtsR in Streptococcus mutans

Cited by 28 publications

References 55 publications

Stress Physiology of Lactic Acid Bacteria

Stress Physiology of Lactic Acid Bacteria

SMU.746-SMU.747, a Putative Membrane Permease Complex, Is Involved in Aciduricity, Acidogenesis, and Biofilm Formation in Streptococcus mutans

Strain-Dependent Recognition of a Unique Degradation Motif by ClpXP in Streptococcus mutans

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