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

Samuel R. Dix, Hayley J. Owen, Ruyue Sun, Asma Ahmad, Sravanthi Shastri, Helena L. Spiewak, Daniel J. Mosby, Matthew J. Harris, Sarah L. Batters, Thomas A. Brooker, Svetomir B. Tzokov, Svetlana E. Sedelnikova, Patrick J. Baker, Per A. Bullough, David W. Rice () and Mark S. Thomas ()
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Samuel R. Dix: University of Sheffield
Hayley J. Owen: University of Sheffield
Ruyue Sun: University of Sheffield Medical School
Asma Ahmad: University of Sheffield Medical School
Sravanthi Shastri: University of Sheffield Medical School
Helena L. Spiewak: University of Sheffield Medical School
Daniel J. Mosby: University of Sheffield Medical School
Matthew J. Harris: University of Sheffield
Sarah L. Batters: University of Sheffield Medical School
Thomas A. Brooker: University of Sheffield Medical School
Svetomir B. Tzokov: University of Sheffield
Svetlana E. Sedelnikova: University of Sheffield
Patrick J. Baker: University of Sheffield
Per A. Bullough: University of Sheffield
David W. Rice: University of Sheffield
Mark S. Thomas: University of Sheffield Medical School

Nature Communications, 2018, vol. 9, issue 1, 1-16

Abstract: 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.

Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07247-1

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DOI: 10.1038/s41467-018-07247-1

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