The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.

The Clp ATPases (Hsp100) constitute a family of closely related proteins that have protein reactivating and remodelling activities typical of molecular chaperones. In Staphylococcus aureus the ClpX chaperone is essential for virulence and for transcription of spa encoding Protein A. The present stud...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Lotte Jelsbak, Hanne Ingmer, Lukás Valihrach, Marianne Thorup Cohn, Mie H G Christiansen, Birgitte H Kallipolitis, Dorte Frees
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/80f361bf29144516a216bd4005cb72c7
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:80f361bf29144516a216bd4005cb72c7
record_format	dspace
spelling	oai:doaj.org-article:80f361bf29144516a216bd4005cb72c72021-11-18T06:35:11ZThe chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.1932-620310.1371/journal.pone.0012752https://doaj.org/article/80f361bf29144516a216bd4005cb72c72010-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20856878/?tool=EBIhttps://doaj.org/toc/1932-6203The Clp ATPases (Hsp100) constitute a family of closely related proteins that have protein reactivating and remodelling activities typical of molecular chaperones. In Staphylococcus aureus the ClpX chaperone is essential for virulence and for transcription of spa encoding Protein A. The present study was undertaken to elucidate the mechanism by which ClpX stimulates expression of Protein A. For this purpose, we prepared antibodies directed against Rot, an activator of spa transcription, and demonstrated that cells devoid of ClpX contain three-fold less Rot than wild-type cells. By varying Rot expression from an inducible promoter we showed that expression of Protein A requires a threshold level of Rot. In the absence of ClpX the Rot content is reduced below this threshold level, hence, explaining the substantially reduced Protein A expression in the clpX mutant. Experiments addressed at pinpointing the role of ClpX in Rot synthesis revealed that ClpX is required for translation of Rot. Interestingly, translation of the spa mRNA was, like the rot mRNA, enhanced by ClpX. These data demonstrate that ClpX performs dual roles in regulating Protein A expression, as ClpX stimulates transcription of spa by enhancing translation of Rot, and that ClpX additionally is required for full translation of the spa mRNA. The current findings emphasize that ClpX has a central role in fine-tuning virulence regulation in S. aureus.Lotte JelsbakHanne IngmerLukás ValihrachMarianne Thorup CohnMie H G ChristiansenBirgitte H KallipolitisDorte FreesPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 9, p e12752 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Lotte Jelsbak Hanne Ingmer Lukás Valihrach Marianne Thorup Cohn Mie H G Christiansen Birgitte H Kallipolitis Dorte Frees The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.
description	The Clp ATPases (Hsp100) constitute a family of closely related proteins that have protein reactivating and remodelling activities typical of molecular chaperones. In Staphylococcus aureus the ClpX chaperone is essential for virulence and for transcription of spa encoding Protein A. The present study was undertaken to elucidate the mechanism by which ClpX stimulates expression of Protein A. For this purpose, we prepared antibodies directed against Rot, an activator of spa transcription, and demonstrated that cells devoid of ClpX contain three-fold less Rot than wild-type cells. By varying Rot expression from an inducible promoter we showed that expression of Protein A requires a threshold level of Rot. In the absence of ClpX the Rot content is reduced below this threshold level, hence, explaining the substantially reduced Protein A expression in the clpX mutant. Experiments addressed at pinpointing the role of ClpX in Rot synthesis revealed that ClpX is required for translation of Rot. Interestingly, translation of the spa mRNA was, like the rot mRNA, enhanced by ClpX. These data demonstrate that ClpX performs dual roles in regulating Protein A expression, as ClpX stimulates transcription of spa by enhancing translation of Rot, and that ClpX additionally is required for full translation of the spa mRNA. The current findings emphasize that ClpX has a central role in fine-tuning virulence regulation in S. aureus.
format	article
author	Lotte Jelsbak Hanne Ingmer Lukás Valihrach Marianne Thorup Cohn Mie H G Christiansen Birgitte H Kallipolitis Dorte Frees
author_facet	Lotte Jelsbak Hanne Ingmer Lukás Valihrach Marianne Thorup Cohn Mie H G Christiansen Birgitte H Kallipolitis Dorte Frees
author_sort	Lotte Jelsbak
title	The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.
title_short	The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.
title_full	The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.
title_fullStr	The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.
title_full_unstemmed	The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.
title_sort	chaperone clpx stimulates expression of staphylococcus aureus protein a by rot dependent and independent pathways.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/80f361bf29144516a216bd4005cb72c7
work_keys_str_mv	AT lottejelsbak thechaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT hanneingmer thechaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT lukasvalihrach thechaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT mariannethorupcohn thechaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT miehgchristiansen thechaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT birgittehkallipolitis thechaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT dortefrees thechaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT lottejelsbak chaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT hanneingmer chaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT lukasvalihrach chaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT mariannethorupcohn chaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT miehgchristiansen chaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT birgittehkallipolitis chaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways AT dortefrees chaperoneclpxstimulatesexpressionofstaphylococcusaureusproteinabyrotdependentandindependentpathways
_version_	1718424490196598784

The chaperone ClpX stimulates expression of Staphylococcus aureus protein A by Rot dependent and independent pathways.

Ejemplares similares