The Streptococcus pneumoniae yefM-yoeB and relBE Toxin-Antitoxin Operons Participate in Oxidative Stress and Biofilm Formation

Chan, Wai Ting; Domenech, Mirian; Moreno-Córdoba, Inmaculada; Navarro-Martínez, Verónica; Nieto, Concha; Moscoso, Miriam; Garcı́a, Ernesto; Espinosa, Manuel

doi:10.3390/toxins10090378

Cited by 37 publications

(48 citation statements)

References 76 publications

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“…Gram-positive bacteria also encode YoeB-YefM TA systems. In Streptococcus pneumoniae, a chromosomal YoeB module is toxic when expressed in E. coli and has been associated with tolerance to oxidative stress and contributions to biofilm formation in its native host (Nieto et al, 2007;Chan et al, 2018). This toxicity is similar to results obtained with the highly similar YoeB-YefM system from Streptococcus suis (Zheng et al, 2015).…”

Section: Introductionsupporting

confidence: 75%

Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins

et al. 2020

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The ribosome-dependent E. coli (Ec) mRNase toxin YoeB has been demonstrated to protect cells during thermal stress. Agrobacterium tumefaciens (At), a plant pathogen, also encodes a YoeB toxin. Initial studies indicated that AtYoeB does not impact the growth of Ec, but its expression is toxic to the native host At. The current work examines this species-specific effect. We establish the highly similar structure and function of Ec and AtYoeB toxins, including the ability of the AtYoeB toxin to inhibit Ec ribosomes in vitro. Comparison of YoeB sequences and structures highlights a four-residue helix between β-strands 2 and 3 that interacts with mRNA bases within the ribosome. This helix sequence is varied among YoeB toxins, and this variation correlates with bacterial classes of proteobacteria. When the four amino acid sequence of this helix is transplanted from EcYoeB onto AtYoeB, the resulting chimera gains toxicity to Ec cells and lessens toxicity to At cells. The reverse is also true, such that EcYoeB with the AtYoeB helix sequence is less toxic to Ec and gains toxicity to At cultures. We suggest this helix sequence directs mRNA sequence-specific degradation, which varies among proteobacterial classes, and thus controls growth inhibition and YoeB toxicity.

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Section: Introductionsupporting

confidence: 75%

Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins

et al. 2020

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“…This study found, first, that the RelBE2 complex positively regulates the promoter activity ( Figure 6 B), while the RelBE of other bacteria negatively regulates the promoter activity [ 49 , 53 , 60 , 61 ]. Considering that type II TA systems contribute to the formation of persistence cells, stress response, biofilm formation and other various biological processes [ 13 , 15 , 31 , 62 , 63 , 64 ], the mechanism of three TA systems in S. suis 2 remains to be further explored in future studies.…”

Section: Discussionmentioning

confidence: 99%

Identification of Three Type II Toxin-Antitoxin Systems in Streptococcus suis Serotype 2

Zhang

Cao

et al. 2018

Toxins

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Type II toxin-antitoxin (TA) systems are highly prevalent in bacterial genomes and have been extensively studied. These modules involve in the formation of persistence cells, the biofilm formation, and stress resistance, which might play key roles in pathogen virulence. SezAT and yefM-yoeB TA modules in Streptococcus suis serotype 2 (S. suis 2) have been studied, although the other TA systems have not been identified. In this study, we investigated nine putative type II TA systems in the genome of S. suis 2 strain SC84 by bioinformatics analysis and identified three of them (two relBE loci and one parDE locus) that function as typical type II TA systems. Interestingly, we found that the introduction of the two RelBE TA systems into Escherichia coli or the induction of the ParE toxin led to cell filamentation. Promoter activity assays indicated that RelB1, RelB2, ParD, and ParDE negatively autoregulated the transcriptions of their respective TA operons, while RelBE2 positively autoregulated its TA operon transcription. Collectively, we identified three TA systems in S. suis 2, and our findings have laid an important foundation for further functional studies on these TA systems.

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“…Deletion of yefM-yoeB, relBE or all TA systems in strain R6 sensitizes these bacteria to oxidative stress; in addition, biofilm formation is significantly impaired, though the growth rate is not significantly affected. These results indicate that two pairs of TA systems in pneumococci perform the same role, similarly contributing to bacterial oxidative stress and biofilm formation [44]. Therefore, we can speculate that when environmental stressors are removed, the newly synthesized antitoxin of a pathogen TA system will complex with the existing cognate or a different source of toxin to reverse toxicity, restore normal growth, and promote adaptation.…”

Section: A Type II Ta System Cross-regulates the Transcription Of Itsmentioning

confidence: 92%

The interplay of the type II TA system with other processes

Wei

Zhong

Min

2019

Preprint

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The type II toxin antitoxin (TA) system is the most well-studied TA system and is widely distributed in bacteria, especially pathogens such as Mycobacterium tuberculosis. Type II TA system plays an important role in many cellular processes, including maintaining the stability of mobile genetic elements, and bacterial altruistic suicide in response to nutritional starvation, environmental stress and phage infection. Interactions between toxin proteins and antitoxin proteins are critical for the regulation and function of type II TA systems; indeed, the understanding of their function is mainly derived from interaction and regulation of paired TA system proteins. Nonetheless, investigating interaction between unpaired TA system proteins, and the interaction between TA system proteins and other functional proteins, are becoming more common and have provided new insight into the complexity of its regulatory mechanism. In this review, we outlined the cross-interaction between TA system proteins, and the interaction between TA system proteins and other functional proteins, and we are trying to explain novel mechanism of TA system in the regulation of cellular activities. On this basis, we further discussed the knowledge and physiological implications of the relevant aspects of TA system research.

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The Streptococcus pneumoniae yefM-yoeB and relBE Toxin-Antitoxin Operons Participate in Oxidative Stress and Biofilm Formation

Cited by 37 publications

References 76 publications

Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins

Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins

Identification of Three Type II Toxin-Antitoxin Systems in Streptococcus suis Serotype 2

The interplay of the type II TA system with other processes

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