An Alternative Terminal Step of the General Secretory Pathway in <named-content content-type="genus-species">Staphylococcus aureus</named-content>

ABSTRACT Type I signal peptidase (SPase) is essential for viability in wild-type bacteria because the terminal step of the bacterial general secretory pathway requires its proteolytic activity to release proteins from their membrane-bound N-terminal leader sequences after translocation across the cy...

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Autores principales:	Arryn Craney, Melissa M. Dix, Ramkrishna Adhikary, Benjamin F. Cravatt, Floyd E. Romesberg
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2015
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/08c0d951e2bf43b6b656e4227aded9c8
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spelling	oai:doaj.org-article:08c0d951e2bf43b6b656e4227aded9c82021-11-15T15:41:27ZAn Alternative Terminal Step of the General Secretory Pathway in <named-content content-type="genus-species">Staphylococcus aureus</named-content>10.1128/mBio.01178-152150-7511https://doaj.org/article/08c0d951e2bf43b6b656e4227aded9c82015-09-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.01178-15https://doaj.org/toc/2150-7511ABSTRACT Type I signal peptidase (SPase) is essential for viability in wild-type bacteria because the terminal step of the bacterial general secretory pathway requires its proteolytic activity to release proteins from their membrane-bound N-terminal leader sequences after translocation across the cytoplasmic membrane. Here, we identify the Staphylococcus aureus operon ayrRABC (SA0337 to SA0340) and show that once released from repression by AyrR, the protein products AyrABC together confer resistance to the SPase inhibitor arylomycin M131 by providing an alternate and novel method of releasing translocated proteins. Thus, the derepression of ayrRABC allows cells to bypass the essentiality of SPase. We demonstrate that AyrABC functionally complements SPase by mediating the processing of the normally secreted proteins, albeit in some cases with reduced efficiency and either without cleavage or via cleavage at a site N-terminal to the canonical SPase cleavage site. Thus, ayrRABC encodes a secretion stress-inducible alternate terminal step of the general secretory pathway.IMPORTANCE Addressing proteins for proper localization within or outside a cell in both eukaryotes and prokaryotes is often accomplished with intrinsic signals which mediate membrane translocation and which ultimately must be removed. The canonical enzyme responsible for the removal of translocation signals is bacterial type I signal peptidase (SPase), which functions at the terminal step of the general secretory pathway and is thus essential in wild-type bacteria. Here, we identify a four-gene operon in S. aureus that encodes an alternate terminal step of the general secretory pathway and thus makes SPase nonessential. The results have important implications for protein secretion in bacteria and potentially for protein trafficking in prokaryotes and eukaryotes in general.Arryn CraneyMelissa M. DixRamkrishna AdhikaryBenjamin F. CravattFloyd E. RomesbergAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 6, Iss 4 (2015)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Arryn Craney Melissa M. Dix Ramkrishna Adhikary Benjamin F. Cravatt Floyd E. Romesberg An Alternative Terminal Step of the General Secretory Pathway in <named-content content-type="genus-species">Staphylococcus aureus</named-content>
description	ABSTRACT Type I signal peptidase (SPase) is essential for viability in wild-type bacteria because the terminal step of the bacterial general secretory pathway requires its proteolytic activity to release proteins from their membrane-bound N-terminal leader sequences after translocation across the cytoplasmic membrane. Here, we identify the Staphylococcus aureus operon ayrRABC (SA0337 to SA0340) and show that once released from repression by AyrR, the protein products AyrABC together confer resistance to the SPase inhibitor arylomycin M131 by providing an alternate and novel method of releasing translocated proteins. Thus, the derepression of ayrRABC allows cells to bypass the essentiality of SPase. We demonstrate that AyrABC functionally complements SPase by mediating the processing of the normally secreted proteins, albeit in some cases with reduced efficiency and either without cleavage or via cleavage at a site N-terminal to the canonical SPase cleavage site. Thus, ayrRABC encodes a secretion stress-inducible alternate terminal step of the general secretory pathway.IMPORTANCE Addressing proteins for proper localization within or outside a cell in both eukaryotes and prokaryotes is often accomplished with intrinsic signals which mediate membrane translocation and which ultimately must be removed. The canonical enzyme responsible for the removal of translocation signals is bacterial type I signal peptidase (SPase), which functions at the terminal step of the general secretory pathway and is thus essential in wild-type bacteria. Here, we identify a four-gene operon in S. aureus that encodes an alternate terminal step of the general secretory pathway and thus makes SPase nonessential. The results have important implications for protein secretion in bacteria and potentially for protein trafficking in prokaryotes and eukaryotes in general.
format	article
author	Arryn Craney Melissa M. Dix Ramkrishna Adhikary Benjamin F. Cravatt Floyd E. Romesberg
author_facet	Arryn Craney Melissa M. Dix Ramkrishna Adhikary Benjamin F. Cravatt Floyd E. Romesberg
author_sort	Arryn Craney
title	An Alternative Terminal Step of the General Secretory Pathway in <named-content content-type="genus-species">Staphylococcus aureus</named-content>
title_short	An Alternative Terminal Step of the General Secretory Pathway in <named-content content-type="genus-species">Staphylococcus aureus</named-content>
title_full	An Alternative Terminal Step of the General Secretory Pathway in <named-content content-type="genus-species">Staphylococcus aureus</named-content>
title_fullStr	An Alternative Terminal Step of the General Secretory Pathway in <named-content content-type="genus-species">Staphylococcus aureus</named-content>
title_full_unstemmed	An Alternative Terminal Step of the General Secretory Pathway in <named-content content-type="genus-species">Staphylococcus aureus</named-content>
title_sort	alternative terminal step of the general secretory pathway in <named-content content-type="genus-species">staphylococcus aureus</named-content>
publisher	American Society for Microbiology
publishDate	2015
url	https://doaj.org/article/08c0d951e2bf43b6b656e4227aded9c8
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An Alternative Terminal Step of the General Secretory Pathway in <named-content content-type="genus-species">Staphylococcus aureus</named-content>

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