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Crystal structure of archaeal toxin-antitoxin RelE–RelB complex with implications for toxin activity and antitoxin effects

Nature Structural & Molecular Biology volume 12, pages 327–331 (2005)Cite this article

Abstract

The Escherichia coli chromosome encodes toxin-antitoxin pairs. The toxin RelE cleaves mRNA positioned at the A-site in ribosomes, whereas the antitoxin RelB relieves the effect of RelE. The hyperthermophilic archaeon Pyrococcus horikoshii OT3 has the archaeal homologs aRelE and aRelB. Here we report the crystal structure of aRelE in complex with aRelB determined at a resolution of 2.3 Å. aRelE folds into an α/β structure, whereas aRelB lacks a distinct hydrophobic core and extensively wraps around the molecular surface of aRelE. Neither component shows structural homology to known ribonucleases or their inhibitors. Site-directed mutagenesis suggests that Arg85, in the C-terminal region, is strongly involved in the functional activity of aRelE, whereas Arg40, Leu48, Arg58 and Arg65 play a modest role in the toxin's activity.

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Figure 1: Structures of aRelB and aRelE.
Figure 2: Gel filtration chromatography of aRelB–aRelE and aRelE.
Figure 3: View of the heterodimer interface between aRelB and aRelE.
Figure 4: Characterization of aRelE mutants.

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Acknowledgements

We thank N. Shimizu (Japan Synchrotron Radiation Research Institute) for help with data collection using synchrotron radiation at beamline BL40B2. We are grateful to M. Ohara (Fukuoka) for helpful comments on the manuscript. This work was supported in part by a grant from the National Project on Protein Structural and Functional Analyses from the Japan Ministry of Education, Culture, Sports, Science and Technology.

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Authors and Affiliations

  1. Department of Bioscience and Biotechnology, Laboratory of Biochemistry, Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka, 812-8581, Japan

    Hisanori Takagi, Yoshimitsu Kakuta, Takahiro Okada & Makoto Kimura

  2. Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, 060-0810, Japan

    Min Yao & Isao Tanaka

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  1. Hisanori Takagi
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Correspondence to Makoto Kimura.

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Supplementary information

Supplementary Fig. 1

Viable count. (PDF 53 kb)

Supplementary Fig. 2

Sequence comparison. (PDF 28 kb)

Supplementary Table 1

Major interactions. (PDF 20 kb)

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Takagi, H., Kakuta, Y., Okada, T. et al. Crystal structure of archaeal toxin-antitoxin RelE–RelB complex with implications for toxin activity and antitoxin effects. Nat Struct Mol Biol 12, 327–331 (2005). https://doi.org/10.1038/nsmb911

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