Structural insights into the function of type VI secretion system TssA subunits.

Abstract

The type VI secretion system (T6SS) is a multi-protein complex that injects bacterial effector proteins into target cells. It is composed of a cell membrane complex anchored to a contractile bacteriophage tail-like apparatus consisting of a sharpened tube that is ejected by the contraction of a sheath against a baseplate. We present structural and biochemical studies on TssA subunits from two different T6SSs that reveal radically different quaternary structures in comparison to the dodecameric E. coli TssA that arise from differences in their C-terminal sequences. Despite this, the different TssAs retain equivalent interactions with other components of the complex and position their highly conserved N-terminal ImpA_N domain at the same radius from the centre of the sheath as a result of their distinct domain architectures, which includes additional spacer domains and highly mobile interdomain linkers. Together, these variations allow these distinct TssAs to perform a similar function in the complex.

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Item Type:	Article
Authors/Creators:	Dix, S.R. https://orcid.org/0000-0002-6907-1435 Owen, H.J. Sun, R. https://orcid.org/0000-0003-3192-7290 Ahmad, A. Shastri, S. Spiewak, H.L. https://orcid.org/0000-0003-1039-5520 Mosby, D.J. Harris, M.J. Batters, S.L. Brooker, T.A. Tzokov, S.B. https://orcid.org/0000-0001-7256-5279 Sedelnikova, S.E. Baker, P.J. https://orcid.org/0000-0003-1995-5643 Bullough, P.A. Rice, D.W. https://orcid.org/0000-0002-7811-0539 Thomas, M.S. https://orcid.org/0000-0003-0701-2584
Copyright, Publisher and Additional Information:	© The Author(s) 2018. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/.
Keywords:	Protein translocation; X-ray crystallography
Dates:	Published: 12 November 2018 Published (online): 12 November 2018 Accepted: 23 October 2018
Institution:	The University of Sheffield
Academic Units:	The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) The University of Sheffield > Sheffield Teaching Hospitals
Depositing User:	Symplectic Sheffield
Date Deposited:	21 Nov 2018 13:49
Last Modified:	21 Nov 2018 13:49
Published Version:	https://doi.org/10.1038/s41467-018-07247-1
Status:	Published
Publisher:	Nature Research
Refereed:	Yes
Identification Number:	10.1038/s41467-018-07247-1
Related URLs:	PubMed URL
Open Archives Initiative ID (OAI ID):	oai:eprints.whiterose.ac.uk:138792

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Structural insights into the function of type VI secretion system TssA subunits.

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