Structural Mechanism of Transcriptional Autorepression of the Escherichia coli RelB/RelE Antitoxin/Toxin Module

Li, Guangyao; Zhang, Yonglong; Inouye, Masayori; Ikura, Mitsuhiko

doi:10.1016/j.jmb.2008.04.039

Cited by 83 publications

(108 citation statements)

References 45 publications

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“…Unfolded antitoxin structures have been reported to be related to their vulnerability to proteolytic degradation (7,42,43). Similarly, CD analyses on HP0895 and HP0895Ctp suggest that the unbound HP0895 antitoxin has a folded core and an unfolded C-terminal tail, as has been reported for RelB (38). The comparison of HP0894 with its structural homologues indicated that some of catalytic residues involved in RNase activity in RNase Sa and YoeB are conserved in HP0894 (Fig.…”

Section: Discussionmentioning

confidence: 54%

“…It has been suggested that the YafQ-DinJ complex comprises two toxin and two antitoxin molecules (39). Dimerization of antitoxins can be related to observations showing that the antitoxins regulate the TA operon by interacting with DNA as homodimers (7,38,40,41). Based on those two differences, we suggest that the HP0895 antitoxin may interact with DNA in a manner different from those adopted by the other, above described antitoxins.…”

Section: Discussionmentioning

confidence: 73%

“…In addition, in the absence of HP0894 toxin and even in the HP0894-HP0895 complex, the HP0895 antitoxin exists as a relatively larger multimer or in an aggregated form rather than a dimer. In contrast, the antitoxins in the RelE-RelB (n ϭ 2), aRelE-aRelB (n ϭ 2), YoeBYefM (n ϭ 1), and MazF-MazE (n ϭ 4) complexes form dimers (toxin n -antitoxin 2 (7,12,21,38)). It has been suggested that the YafQ-DinJ complex comprises two toxin and two antitoxin molecules (39).…”

Section: Discussionmentioning

confidence: 99%

“…In the absence of toxins, native RelB, YefM, and aRelB antitoxins are regarded as being completely unfolded proteins or as having partially unfolded structures in their C-terminal regions (7,8,38,(41)(42)(43)(44). Unfolded antitoxin structures have been reported to be related to their vulnerability to proteolytic degradation (7,42,43).…”

Section: Discussionmentioning

confidence: 99%

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Functional Identification of Toxin-Antitoxin Molecules from Helicobacter pylori 26695 and Structural Elucidation of the Molecular Interactions

Han

Matsuura

Ahn

et al. 2011

Journal of Biological Chemistry

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Bacterial toxin-antitoxin (TA) systems are associated with many important cellular processes including antibiotic resistance and microorganism virulence. Here, we identify and structurally characterize TA molecules from the gastric pathogen, Helicobacter pylori. The HP0894 protein had been previously suggested, through our structural genomics approach, to be a putative toxin molecule. In this study, the intrinsic RNase activity and the bacterial cell growth-arresting activity of HP0894 were established. 85-Lys 87 were observed to be the main contributors to sequence recognition. The action of HP0894 could be inhibited by the HP0895 protein, and the HP0894-HP0895 complex formed an oligomer with a binding stoichiometry of 1:1. The N and C termini of HP0894 constituted the binding sites to HP0895. In contrast, the unstructured C-terminal region of HP0895 was responsible for binding to HP0894 and underwent a conformational change in the process. Finally, DNA binding activity was observed for both HP0895 and the HP0894-0895 complex but not for HP0894 alone. Taken together, it is concluded that the HP0894-HP0895 protein couple is a TA system in H. pylori, where HP0894 is a toxin with an RNase function, whereas HP0895 is an antitoxin functioning by binding to both the toxin and DNA.

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Section: Discussionmentioning

confidence: 54%

Section: Discussionmentioning

confidence: 73%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Functional Identification of Toxin-Antitoxin Molecules from Helicobacter pylori 26695 and Structural Elucidation of the Molecular Interactions

Han

Matsuura

Ahn

et al. 2011

Journal of Biological Chemistry

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“…Thus, the dimer would have a ribbon-helix-helix (RHH) motif, by which it would bind to its target DNA, similar to the Arc-CopG-Omega family of transcriptional repressors (37,62,111,121); in fact, the 28 N-terminal amino acids of the pneumococcal RelB protein share 64% similarity with the 45-residue CopG transcriptional repressor encoded by streptococcal plasmid pMV158 (37,105). The RHH DNA-binding motif also seems to be present in the N-terminal regions of the RelB and YefM proteins from E. coli (79,93,119) and in the pneumococcal RelB2 protein (105) but not in the archaeal RelB proteins (53,138) or in the pneumococcal YefM protein (our unpublished observations).…”

Section: Structural Informationmentioning

confidence: 99%

Toxin-Antitoxin Genes of the Gram-Positive Pathogen Streptococcus pneumoniae: So Few and Yet So Many

Chan

Moreno-Córdoba

Yeo

et al. 2012

Microbiol Mol Biol Rev

115

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SUMMARYPneumococcal infections cause up to 2 million deaths annually and raise a large economic burden and thus constitute an important threat to mankind. Because of the increase in the antibiotic resistance ofStreptococcus pneumoniaeclinical isolates, there is an urgent need to find new antimicrobial approaches to triumph over pneumococcal infections. Toxin-antitoxin (TA) systems (TAS), which are present in most living bacteria but not in eukaryotes, have been proposed as an effective strategy to combat bacterial infections. Type II TAS comprise a stable toxin and a labile antitoxin that form an innocuous TA complex under normal conditions. Under stress conditions, TA synthesis will be triggered, resulting in the degradation of the labile antitoxin and the release of the toxin protein, which would poison the host cells. The three functional chromosomal TAS fromS. pneumoniaethat have been studied as well as their molecular characteristics are discussed in detail in this review. Furthermore, a meticulous bioinformatics search has been performed for 48 pneumococcal genomes that are found in public databases, and more putative TAS, homologous to well-characterized ones, have been revealed. Strikingly, several unusual putative TAS, in terms of components and genetic organizations previously not envisaged, have been discovered and are further discussed. Previously, we reported a novel finding in which a unique pneumococcal DNA signature, the BOX element, affected the regulation of the pneumococcalyefM-yoeBTAS. This BOX element has also been found in some of the other pneumococcal TAS. In this review, we also discuss possible relationships between some of the pneumococcal TAS with pathogenicity, competence, biofilm formation, persistence, and an interesting phenomenon called bistability.

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Transcriptional Control of Toxin–Antitoxin Expression: Keeping Toxins Under Wraps Until the Time is Right

Kędzierska

Hayes

2016

Stress and Environmental Regulation of Gene Expression and Adaptation in Bacteria

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Structural Mechanism of Transcriptional Autorepression of the Escherichia coli RelB/RelE Antitoxin/Toxin Module

Cited by 83 publications

References 45 publications

Functional Identification of Toxin-Antitoxin Molecules from Helicobacter pylori 26695 and Structural Elucidation of the Molecular Interactions

Functional Identification of Toxin-Antitoxin Molecules from Helicobacter pylori 26695 and Structural Elucidation of the Molecular Interactions

Toxin-Antitoxin Genes of the Gram-Positive Pathogen Streptococcus pneumoniae: So Few and Yet So Many

Transcriptional Control of Toxin–Antitoxin Expression: Keeping Toxins Under Wraps Until the Time is Right

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