Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS

Rhys Alexander Dunstan, Eva Heinz, Lakshmi Carmel Wijeyewickrema, Robert Neil Pike, Anthony Wayne Purcell, Timothy J Evans, Judyta Praszkier, Roy Michael Robins-Browne, Richard Anthony Strugnell, Konstantin V Korotkov, Trevor James Lithgow

Research output: Contribution to journalArticleResearchpeer-review

41 Citations (Scopus)

Abstract

The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. A key element in the machinery is the secretin: an integral, multimeric outer membrane protein that forms the secretion pore. We show that three distinct forms of T2SSs can be distinguished based on the sequence characteristics of their secretin pores. Detailed comparative analysis of two of these, the Klebsiella-type and Vibrio-type, showed them to be further distinguished by the pilotin that mediates their transport and assembly into the outer membrane. We have determined the crystal structure of the novel pilotin AspS from Vibrio cholerae, demonstrating convergent evolution wherein AspS is functionally equivalent and yet structurally unrelated to the pilotins found in Klebsiella and other bacteria. AspS binds to a specific targeting sequence in the Vibrio-type secretins, enhances the kinetics of secretin assembly, and homologs of AspS are found in all species of Vibrio as well those few strains of Escherichia and Shigella that have acquired a Vibrio-type T2SS.
Original languageEnglish
Pages (from-to)1 - 14
Number of pages14
JournalPLoS Pathogens
Volume9
Issue number1 (Art # e1003117)
DOIs
Publication statusPublished - 2013

Cite this

Dunstan, Rhys Alexander ; Heinz, Eva ; Wijeyewickrema, Lakshmi Carmel ; Pike, Robert Neil ; Purcell, Anthony Wayne ; Evans, Timothy J ; Praszkier, Judyta ; Robins-Browne, Roy Michael ; Strugnell, Richard Anthony ; Korotkov, Konstantin V ; Lithgow, Trevor James. / Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS. In: PLoS Pathogens. 2013 ; Vol. 9, No. 1 (Art # e1003117). pp. 1 - 14.
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abstract = "The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. A key element in the machinery is the secretin: an integral, multimeric outer membrane protein that forms the secretion pore. We show that three distinct forms of T2SSs can be distinguished based on the sequence characteristics of their secretin pores. Detailed comparative analysis of two of these, the Klebsiella-type and Vibrio-type, showed them to be further distinguished by the pilotin that mediates their transport and assembly into the outer membrane. We have determined the crystal structure of the novel pilotin AspS from Vibrio cholerae, demonstrating convergent evolution wherein AspS is functionally equivalent and yet structurally unrelated to the pilotins found in Klebsiella and other bacteria. AspS binds to a specific targeting sequence in the Vibrio-type secretins, enhances the kinetics of secretin assembly, and homologs of AspS are found in all species of Vibrio as well those few strains of Escherichia and Shigella that have acquired a Vibrio-type T2SS.",
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Dunstan, RA, Heinz, E, Wijeyewickrema, LC, Pike, RN, Purcell, AW, Evans, TJ, Praszkier, J, Robins-Browne, RM, Strugnell, RA, Korotkov, KV & Lithgow, TJ 2013, 'Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS', PLoS Pathogens, vol. 9, no. 1 (Art # e1003117), pp. 1 - 14. https://doi.org/10.1371/journal.ppat.1003117

Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS. / Dunstan, Rhys Alexander; Heinz, Eva; Wijeyewickrema, Lakshmi Carmel; Pike, Robert Neil; Purcell, Anthony Wayne; Evans, Timothy J; Praszkier, Judyta; Robins-Browne, Roy Michael; Strugnell, Richard Anthony; Korotkov, Konstantin V; Lithgow, Trevor James.

In: PLoS Pathogens, Vol. 9, No. 1 (Art # e1003117), 2013, p. 1 - 14.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Purcell, Anthony Wayne

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AU - Korotkov, Konstantin V

AU - Lithgow, Trevor James

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N2 - The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. A key element in the machinery is the secretin: an integral, multimeric outer membrane protein that forms the secretion pore. We show that three distinct forms of T2SSs can be distinguished based on the sequence characteristics of their secretin pores. Detailed comparative analysis of two of these, the Klebsiella-type and Vibrio-type, showed them to be further distinguished by the pilotin that mediates their transport and assembly into the outer membrane. We have determined the crystal structure of the novel pilotin AspS from Vibrio cholerae, demonstrating convergent evolution wherein AspS is functionally equivalent and yet structurally unrelated to the pilotins found in Klebsiella and other bacteria. AspS binds to a specific targeting sequence in the Vibrio-type secretins, enhances the kinetics of secretin assembly, and homologs of AspS are found in all species of Vibrio as well those few strains of Escherichia and Shigella that have acquired a Vibrio-type T2SS.

AB - The Type II Secretion System (T2SS) is a molecular machine that drives the secretion of fully-folded protein substrates across the bacterial outer membrane. A key element in the machinery is the secretin: an integral, multimeric outer membrane protein that forms the secretion pore. We show that three distinct forms of T2SSs can be distinguished based on the sequence characteristics of their secretin pores. Detailed comparative analysis of two of these, the Klebsiella-type and Vibrio-type, showed them to be further distinguished by the pilotin that mediates their transport and assembly into the outer membrane. We have determined the crystal structure of the novel pilotin AspS from Vibrio cholerae, demonstrating convergent evolution wherein AspS is functionally equivalent and yet structurally unrelated to the pilotins found in Klebsiella and other bacteria. AspS binds to a specific targeting sequence in the Vibrio-type secretins, enhances the kinetics of secretin assembly, and homologs of AspS are found in all species of Vibrio as well those few strains of Escherichia and Shigella that have acquired a Vibrio-type T2SS.

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