Higher-Order Structure in Bacterial VapBC Toxin-Antitoxin Complexes

Kirstine L Bendtsen; Ditlev E Brodersen

doi:10.1007/978-3-319-46503-6_14

Higher-Order Structure in Bacterial VapBC Toxin-Antitoxin Complexes

7 Citations (Scopus)

Abstract

Toxin-antitoxin systems are widespread in the bacterial kingdom, including in pathogenic species, where they allow rapid adaptation to changing environmental conditions through selective inhibition of key cellular processes, such as DNA replication or protein translation. Under normal growth conditions, type II toxins are inhibited through tight protein-protein interaction with a cognate antitoxin protein. This toxin-antitoxin complex associates into a higher-order macromolecular structure, typically heterotetrameric or heterooctameric, exposing two DNA binding domains on the antitoxin that allow auto-regulation of transcription by direct binding to promoter DNA. In this chapter, we review our current understanding of the structural characteristics of type II toxin-antitoxin complexes in bacterial cells, with a special emphasis on the staggering variety of higher-order architecture observed among members of the VapBC family. This structural variety is a result of poor conservation at the primary sequence level and likely to have signiﬁcant and functional implications on the way toxin-antitoxin expression is regulated.

Original language	English
Title of host publication	Macromolecular Protein Complexes
Number of pages	32
Volume	83
Publisher	Springer
Publication date	2017
Pages	381-412
DOIs	https://doi.org/10.1007/978-3-319-46503-6_14
Publication status	Published - 2017

Series	Subcellular biochemistry
ISSN	0306-0225

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abstract = "Toxin-antitoxin systems are widespread in the bacterial kingdom, including in pathogenic species, where they allow rapid adaptation to changing environmental conditions through selective inhibition of key cellular processes, such as DNA replication or protein translation. Under normal growth conditions, type II toxins are inhibited through tight protein-protein interaction with a cognate antitoxin protein. This toxin-antitoxin complex associates into a higher-order macromolecular structure, typically heterotetrameric or heterooctameric, exposing two DNA binding domains on the antitoxin that allow auto-regulation of transcription by direct binding to promoter DNA. In this chapter, we review our current understanding of the structural characteristics of type II toxin-antitoxin complexes in bacterial cells, with a special emphasis on the staggering variety of higher-order architecture observed among members of the VapBC family. This structural variety is a result of poor conservation at the primary sequence level and likely to have signiﬁcant and functional implications on the way toxin-antitoxin expression is regulated.",

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AB - Toxin-antitoxin systems are widespread in the bacterial kingdom, including in pathogenic species, where they allow rapid adaptation to changing environmental conditions through selective inhibition of key cellular processes, such as DNA replication or protein translation. Under normal growth conditions, type II toxins are inhibited through tight protein-protein interaction with a cognate antitoxin protein. This toxin-antitoxin complex associates into a higher-order macromolecular structure, typically heterotetrameric or heterooctameric, exposing two DNA binding domains on the antitoxin that allow auto-regulation of transcription by direct binding to promoter DNA. In this chapter, we review our current understanding of the structural characteristics of type II toxin-antitoxin complexes in bacterial cells, with a special emphasis on the staggering variety of higher-order architecture observed among members of the VapBC family. This structural variety is a result of poor conservation at the primary sequence level and likely to have signiﬁcant and functional implications on the way toxin-antitoxin expression is regulated.

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Higher-Order Structure in Bacterial VapBC Toxin-Antitoxin Complexes

Abstract

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