The kis and kid genes of the parD maintenance system of plasmid R1 form an operon that is autoregulated at the level of transcription by the co‐ordinated action of the Kis and Kid proteins

Ruiz-Echevarría, María J.; Berzal‐Herranz, Alfredo; Gerdes, Kenn; Dı́az-Orejas, Ramón

doi:10.1111/j.1365-2958.1991.tb01977.x

Cited by 76 publications

(74 citation statements)

References 29 publications

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“…11 The coordinate action of Kid and Kis has been shown to autoregulate parD at the level of transcription. 12 The crystal structure of the Kid protein has been determined, revealing a symmetric dimer. 13,14 and MazE (ChpAI), chromosomal homologues of Kid and Kis, has been described.…”

Section: Introductionmentioning

confidence: 99%

Model for RNA Binding and the Catalytic Site of the RNase Kid of the Bacterial parD Toxin–Antitoxin System

Kamphuis

Bonvin

Monti

et al. 2006

Journal of Molecular Biology

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The toxin Kid and antitoxin Kis are encoded by the parD operon of Escherichia coli plasmid R1. Kid and its chromosomal homologues MazF and ChpBK have been shown to inhibit protein synthesis in cell extracts and to act as ribosome-independent endoribonucleases in vitro. Kid cleaves RNA preferentially at the 5 0 side of the A residue in the nucleotide sequence 5 0 -UA(A/C)-3 0 of single-stranded regions. Here, we show that RNA cleavage by Kid yields two fragments with a 2 0 :3 0 -cyclic phosphate group and a free 5 0 -OH group, respectively. The cleavage mechanism is similar to that of RNases A and T1, involving the uracil 2 0 -OH group. Via NMR titration studies with an uncleavable RNA mimic, we demonstrate that residues of both monomers of the Kid dimer together form a concatenated RNA-binding surface. Docking calculations based on the NMR chemical shifts, the cleavage mechanism and previously reported mutagenesis data provide a detailed picture of the position of the AUACA fragment within the binding pocket. We propose that residues D75, R73 and H17 form the active site of the Kid toxin, where D75 and R73 are the catalytic base and acid, respectively. The RNA sequence specificity is defined by residues T46, S47, A55, F57, T69, V71 and R73. Our data show the importance of these residues for Kid function, and the implications of our results for related toxins, such as MazF, CcdB and RelE, are discussed.

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Section: Introductionmentioning

confidence: 99%

Model for RNA Binding and the Catalytic Site of the RNase Kid of the Bacterial parD Toxin–Antitoxin System

Kamphuis

Bonvin

Monti

et al. 2006

Journal of Molecular Biology

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“…The pemI-pemK system and the kis-kid system are involved in the stable maintenance of two closely related incFII low copy plasmids, plasmid R100 (14,15) and plasmid R1 (10,32), respectively. These two systems turned out to be identical (1).…”

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confidence: 99%

Interference of mRNA Function by Sequence-specific Endoribonuclease PemK

Zhang

Zhu

et al. 2004

Journal of Biological Chemistry

122

149

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In Escherichia coli, programmed cell death is mediated through the system called "addiction module," which consists of a pair of genes encoding a stable toxin and a labile antitoxin. The pemI-pemK system is an addiction module present on plasmid R100. It helps to maintain the plasmid by post-segregational killing in E. coli population. Here we demonstrate that purified PemK, the toxin encoded by the pemI-pemK addiction module, inhibits protein synthesis in an E. coli cell-free system, whereas the addition of PemI, the antitoxin against PemK, resumes the protein synthesis. Further studies reveal that PemK is a sequence-specific endoribonuclease that cleaves mRNAs to inhibit protein synthesis, whereas PemI blocks the endoribonuclease activity of PemK. PemK cleaves only single-stranded RNA preferentially at the 5 or 3 side of the A residue in the "UAH" sequences (where H is C, A, or U). Upon induction, PemK cleaves cellular mRNAs to effectively block protein synthesis in E. coli. The pemK homologue genes have been identified on the genomes of a wide range of bacteria. We propose that PemK and its homologues form a novel endoribonuclease family that interferes with mRNA function by cleaving cellular mRNAs in a sequence-specific manner.In Escherichia coli, programmed cell death is proposed to be mediated through the system called "addiction module," which consists of a pair of genes encoding a toxin and an antitoxin (1). The addiction module has the following properties. (a) The toxic protein is stable, whereas the antitoxin is a labile protein. (b) The toxin and the antitoxin are coexpressed from an operon and interact with each other to form a stable complex. (c) Their expression is auto-regulated either by the toxin-antitoxin complex or by the antitoxin alone. When the co-expression is inhibited under stress conditions, the antitoxin is degraded by proteases, enabling the toxin to act on its target. In E. coli, some extrachromosomal elements are known to contain addiction modules causing the bacterial programmed cell death by the so-called postsegregational killing effect. The most studied extrachromosomal addiction modules are the phd-doc system on bacteriophage P1 (2-5), the ccdA-ccdB system on factor F (6 -9), the kis-kid system on plasmid R1 (10 -13), and the pemIpemK system on plasmid R100 (14 -17). Interestingly, the E. coli chromosome also contains several addiction module systems, such as the relBE system (18 -21), the mazEF system (22-25), and the chpB system (26 -28).The cellular effects of the toxins in the addiction modules have been studied quite extensively. CcdB, the toxin in the ccdA-ccdB system, interacts with DNA gyrase to block DNA replication (7,29), and RelE, the toxin in the relBE system, is not able to degrade free RNA but cleaves mRNA in the ribosome A site with high codon specificity (21). Recently, it was demonstrated that the A-site mRNA cleavage can occur in the absence of RelE (30). The exact mechanism of the A-site mRNA cleavage is still unknown. It has been proposed that MazF (ChpAK)...

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“…The coordinate action of Kid and Kis has been shown to autoregulate parD at the level of transcription [46][47][48][49]. This kind of transcriptional control is generally observed for TA systems.…”

Section: Common Phenomenamentioning

confidence: 99%

“…This kind of transcriptional control is generally observed for TA systems. The antitoxin represses transcription [33,47,[49][50][51] by binding the operator with the N-terminus [48,52,53]. The toxin acts as a corepressor, since the TA complex has a higher DNA-affinity than the antitoxin alone [33,46,53,54].…”

Section: Common Phenomenamentioning

confidence: 99%

Structure and Function of Bacterial Kid-Kis and Related Toxin-Antitoxin Systems

Kamphuis¹,

Monti²,

Heuvel³

et al. 2007

PPL

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Toxin-antitoxin systems were discovered as plasmid auxiliary maintenance cassettes. In recent years, an increasing amount of structural and functional information has become available about the proteins involved, allowing the understanding of bacterial cell growth inhibition by the toxins on a molecular level. A well-studied TA system is formed by the proteins Kid and Kis, encoded by the parD operon of the Escherichia coli plasmid R1. The toxicity of Kid has been related to its endoribonuclease activity, which is counteracted by binding of the antitoxin Kis at the proposed active site. In this review, the structural studies on the Kid-Kis system are compared to those of three related toxin-antitoxin systems: MazF-MazE, CcdB-CcdA and RelE-RelB.

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The kis and kid genes of the parD maintenance system of plasmid R1 form an operon that is autoregulated at the level of transcription by the co‐ordinated action of the Kis and Kid proteins

Cited by 76 publications

References 29 publications

Model for RNA Binding and the Catalytic Site of the RNase Kid of the Bacterial parD Toxin–Antitoxin System

Model for RNA Binding and the Catalytic Site of the RNase Kid of the Bacterial parD Toxin–Antitoxin System

Interference of mRNA Function by Sequence-specific Endoribonuclease PemK

Structure and Function of Bacterial Kid-Kis and Related Toxin-Antitoxin Systems

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