Composition and Activity of the Non-canonical Gram-positive SecY2 Complex*

The accessory Sec system in Streptococcus gordonii DL1 is a specialized export system that transports a large serine-rich repeat protein, Hsa, to the bacterial surface. The system is composed of core proteins SecA2 and SecY2 and accessory Sec proteins Asp1–Asp5. Similar to canonical SecYEG, SecY2 fo...

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Main Authors:	Bandara, Mikaila, Corey, Robin A., Martin, Remy, Skehel, J. Mark, Blocker, Ariel J., Jenkinson, Howard F., Collinson, Ian
Format:	Online
Language:	English
Published:	American Society for Biochemistry and Molecular Biology 2016
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5076819/

id	pubmed-5076819
recordtype	oai_dc
spelling	pubmed-50768192016-10-27 Composition and Activity of the Non-canonical Gram-positive SecY2 Complex* Bandara, Mikaila Corey, Robin A. Martin, Remy Skehel, J. Mark Blocker, Ariel J. Jenkinson, Howard F. Collinson, Ian Membrane Biology The accessory Sec system in Streptococcus gordonii DL1 is a specialized export system that transports a large serine-rich repeat protein, Hsa, to the bacterial surface. The system is composed of core proteins SecA2 and SecY2 and accessory Sec proteins Asp1–Asp5. Similar to canonical SecYEG, SecY2 forms a channel for translocation of the Hsa adhesin across the cytoplasmic membrane. Accessory Sec proteins Asp4 and Asp5 have been suggested to work alongside SecY2 to form the translocon, similar to the associated SecY, SecE, and SecG of the canonical system (SecYEG). To test this theory, S. gordonii secY2, asp4, and asp5 were co-expressed in Escherichia coli. The resultant complex was subsequently purified, and its composition was confirmed by mass spectrometry to be SecY2-Asp4-Asp5. Like SecYEG, the non-canonical complex activates the ATPase activity of the SecA motor (SecA2). This study also shows that Asp4 and Asp5 are necessary for optimal adhesion of S. gordonii to glycoproteins gp340 and fibronectin, known Hsa binding partners, as well as for early stage biofilm formation. This work opens new avenues for understanding the structure and function of the accessory Sec system. American Society for Biochemistry and Molecular Biology 2016-10-07 2016-08-22 /pmc/articles/PMC5076819/ /pubmed/27551046 http://dx.doi.org/10.1074/jbc.M116.729806 Text en © 2016 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version free via Creative Commons CC-BY license (http://creativecommons.org/licenses/by/4.0) .
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Bandara, Mikaila Corey, Robin A. Martin, Remy Skehel, J. Mark Blocker, Ariel J. Jenkinson, Howard F. Collinson, Ian
spellingShingle	Bandara, Mikaila Corey, Robin A. Martin, Remy Skehel, J. Mark Blocker, Ariel J. Jenkinson, Howard F. Collinson, Ian Composition and Activity of the Non-canonical Gram-positive SecY2 Complex*
author_facet	Bandara, Mikaila Corey, Robin A. Martin, Remy Skehel, J. Mark Blocker, Ariel J. Jenkinson, Howard F. Collinson, Ian
author_sort	Bandara, Mikaila
title	Composition and Activity of the Non-canonical Gram-positive SecY2 Complex*
title_short	Composition and Activity of the Non-canonical Gram-positive SecY2 Complex*
title_full	Composition and Activity of the Non-canonical Gram-positive SecY2 Complex*
title_fullStr	Composition and Activity of the Non-canonical Gram-positive SecY2 Complex*
title_full_unstemmed	Composition and Activity of the Non-canonical Gram-positive SecY2 Complex*
title_sort	composition and activity of the non-canonical gram-positive secy2 complex*
description	The accessory Sec system in Streptococcus gordonii DL1 is a specialized export system that transports a large serine-rich repeat protein, Hsa, to the bacterial surface. The system is composed of core proteins SecA2 and SecY2 and accessory Sec proteins Asp1–Asp5. Similar to canonical SecYEG, SecY2 forms a channel for translocation of the Hsa adhesin across the cytoplasmic membrane. Accessory Sec proteins Asp4 and Asp5 have been suggested to work alongside SecY2 to form the translocon, similar to the associated SecY, SecE, and SecG of the canonical system (SecYEG). To test this theory, S. gordonii secY2, asp4, and asp5 were co-expressed in Escherichia coli. The resultant complex was subsequently purified, and its composition was confirmed by mass spectrometry to be SecY2-Asp4-Asp5. Like SecYEG, the non-canonical complex activates the ATPase activity of the SecA motor (SecA2). This study also shows that Asp4 and Asp5 are necessary for optimal adhesion of S. gordonii to glycoproteins gp340 and fibronectin, known Hsa binding partners, as well as for early stage biofilm formation. This work opens new avenues for understanding the structure and function of the accessory Sec system.
publisher	American Society for Biochemistry and Molecular Biology
publishDate	2016
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5076819/
_version_	1613694920114044928

Composition and Activity of the Non-canonical Gram-positive SecY2 Complex*

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