Degradation of SsrA-tagged proteins in streptococci

Tao, Liang; Biswas, Indranil

doi:10.1099/mic.0.000048

Cited by 15 publications

(24 citation statements)

References 60 publications

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“…Key to this important process is the involvement of the ClpXP proteolytic complex. As is the case in other well-studied bacteria such as E. coli and Bacillus subtilis , ClpXP is the major proteolytic complex involved in protein quality control in S. mutans (19, 22, 27). As expected from its role in regulated proteolysis, inactivation of either clpP or clpX leads to pleotropic effects, including defects in biofilm formation, bacteriocin production, and competence development (19, 27).…”

Section: Discussionmentioning

confidence: 95%

“…Furthermore, E. coli ClpXP is known to recognize various C-terminal tags (16). Since the tags that are recognized by E. coli ClpXP are small (three to six residues in length), we attached the last six residues of the DivIVA and SsbA to the green fluorescent protein (GFP), which we had previously found to be suitable for proteolytic studies (22). Addition of the six residues (KLNINE) derived from DivIVA to GFP did not render the protein degradable by ClpXP, whereas the addition of six residues (DDDLPF) derived from SsbA made the GFP susceptible to ClpXP-mediated degradation (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The protein was eluted using a salt gradient of 250 to 1,000 mM NaCl, and the purity of the recovered protein was assessed by SDS-PAGE. S. mutans ClpX was purified as described by Tao and Biswas (22). …”

Section: Methodsmentioning

confidence: 99%

“…The purity of the proteins was assessed by SDS-PAGE. GFP-AVAA was purified as described by Tao and Biswas (22). …”

Section: Methodsmentioning

confidence: 99%

“…Surprisingly, both the clpX and clpP mutant strains displayed improved growth capability under acid stress conditions and showed enhanced viability during long-term survival (20). ClpXP has a pleiotropic effect in S. mutans ; however, the natures of the substrates or the sequences recognized by ClpXP have not been systematically identified, except for a few target proteins such as Spx and IvrR and SsrA-tagged substrates (22–24). In fact, besides E. coli , the exact sequence motifs for ClpXP recognition have not been verified in other organisms.…”

Section: Introductionmentioning

confidence: 99%

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

Jana

Tao

Biswas

2016

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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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Section: Discussionmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

“…The purity of the proteins was assessed by SDS-PAGE. GFP-AVAA was purified as described by Tao and Biswas (22). …”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Jana

Tao

Biswas

2016

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Clp ATPases differentially affect natural competence development in Streptococcus mutans

Pandey

Biswas

2022

MicrobiologyOpen

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In naturally competent bacteria, DNA transformation through horizontal gene transfer is an evolutionary mechanism to receive extracellular DNA. Bacteria need to maintain a state of competence to accept foreign DNA, and this is an energy-driven phenomenon that is tightly controlled. In Streptococcus, competence development is a complex process that is not fully understood. In this study, we used Streptococcus mutans, an oral bacterium, to determine how cell density affects competence development. We found that in S. mutans the transformation efficiency is maximum when the transforming DNA was added at low cell density and incubated for 2.5 h before selecting for transformants. We also found that S. mutans cells remain competent until the mid-logarithmic phase, after which the competence decreases drastically. Surprisingly, we observed that individual components of Clp proteolytic complexes differentially regulate competence. If the transformation is carried out at the early growth phase, both ClpP protease and ClpX ATPase are needed for competence. In contrast, we found that both ClpC and ClpE negatively affect competence. We also found that if the transformation is carried out at the mid-logarithmic growth phase ClpX is still required for competence, but ClpP negatively affects competence. While the exact reason for this differential effect of ClpP and ClpX on transformation is currently unknown, we found that both ClpC and ClpE have a negative effect on transformation, which was not reported before.

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Alanine Tails Signal Proteolysis in Bacterial Ribosome-Associated Quality Control

Lytvynenko

Paternoga

Thrun

et al. 2019

Cell

153

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Degradation of SsrA-tagged proteins in streptococci

Cited by 15 publications

References 60 publications

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

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

Clp ATPases differentially affect natural competence development in Streptococcus mutans

Alanine Tails Signal Proteolysis in Bacterial Ribosome-Associated Quality Control

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