Enterococcus faecalis virulence regulator FsrA binding to target promoters
- Autores
- Del Papa, María Florencia; Perego, Marta
- Año de publicación
- 2011
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The FsrABDC signal transduction system is a major virulence regulator in Enterococcus faecalis. The FsrC sensor histidine kinase, upon activation by the gelatinase biosynthesis-activating pheromone (GBAP) peptide encoded by the fsrBD genes, phosphorylates the FsrA response regulator required for the transcription of the fsrBDC and the gelE-sprE genes from the fsrB promoter and the gelE promoter, respectively. FsrA belongs to the LytTR family of proteins, which includes other virulence regulators, such as AgrA of Staphylococcus aureus, AlgR of Pseudomonas aeruginosa, and VirR of Clostridium perfringens. The LytTR DNA-binding domain that characterizes these proteins generally binds to two imperfect direct repeats separated by a number of bases that place the repeats on the same face of the DNA helix. In this study, we demonstrated that FsrA also binds to two imperfect direct repeats separated by 13 bp, based on the consensus sequence of FsrA, T/AT/CAA/GG GAA/G, which is consistent with the binding characteristics of LytTR domains.
Instituto de Biotecnologia y Biologia Molecular - Materia
-
Biología
Biotecnología
Virulence regulator
Virulencia
Enterococcus faecalis - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/84210
Ver los metadatos del registro completo
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Enterococcus faecalis virulence regulator FsrA binding to target promotersDel Papa, María FlorenciaPerego, MartaBiologíaBiotecnologíaVirulence regulatorVirulenciaEnterococcus faecalisThe FsrABDC signal transduction system is a major virulence regulator in Enterococcus faecalis. The FsrC sensor histidine kinase, upon activation by the gelatinase biosynthesis-activating pheromone (GBAP) peptide encoded by the fsrBD genes, phosphorylates the FsrA response regulator required for the transcription of the fsrBDC and the gelE-sprE genes from the fsrB promoter and the gelE promoter, respectively. FsrA belongs to the LytTR family of proteins, which includes other virulence regulators, such as AgrA of Staphylococcus aureus, AlgR of Pseudomonas aeruginosa, and VirR of Clostridium perfringens. The LytTR DNA-binding domain that characterizes these proteins generally binds to two imperfect direct repeats separated by a number of bases that place the repeats on the same face of the DNA helix. In this study, we demonstrated that FsrA also binds to two imperfect direct repeats separated by 13 bp, based on the consensus sequence of FsrA, T/AT/CAA/GG GAA/G, which is consistent with the binding characteristics of LytTR domains.Instituto de Biotecnologia y Biologia Molecular2011-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf1527-1532http://sedici.unlp.edu.ar/handle/10915/84210enginfo:eu-repo/semantics/altIdentifier/issn/0021-9193info:eu-repo/semantics/altIdentifier/doi/10.1128/jb.01522-10info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T10:48:25Zoai:sedici.unlp.edu.ar:10915/84210Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:48:26.418SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Enterococcus faecalis virulence regulator FsrA binding to target promoters |
title |
Enterococcus faecalis virulence regulator FsrA binding to target promoters |
spellingShingle |
Enterococcus faecalis virulence regulator FsrA binding to target promoters Del Papa, María Florencia Biología Biotecnología Virulence regulator Virulencia Enterococcus faecalis |
title_short |
Enterococcus faecalis virulence regulator FsrA binding to target promoters |
title_full |
Enterococcus faecalis virulence regulator FsrA binding to target promoters |
title_fullStr |
Enterococcus faecalis virulence regulator FsrA binding to target promoters |
title_full_unstemmed |
Enterococcus faecalis virulence regulator FsrA binding to target promoters |
title_sort |
Enterococcus faecalis virulence regulator FsrA binding to target promoters |
dc.creator.none.fl_str_mv |
Del Papa, María Florencia Perego, Marta |
author |
Del Papa, María Florencia |
author_facet |
Del Papa, María Florencia Perego, Marta |
author_role |
author |
author2 |
Perego, Marta |
author2_role |
author |
dc.subject.none.fl_str_mv |
Biología Biotecnología Virulence regulator Virulencia Enterococcus faecalis |
topic |
Biología Biotecnología Virulence regulator Virulencia Enterococcus faecalis |
dc.description.none.fl_txt_mv |
The FsrABDC signal transduction system is a major virulence regulator in Enterococcus faecalis. The FsrC sensor histidine kinase, upon activation by the gelatinase biosynthesis-activating pheromone (GBAP) peptide encoded by the fsrBD genes, phosphorylates the FsrA response regulator required for the transcription of the fsrBDC and the gelE-sprE genes from the fsrB promoter and the gelE promoter, respectively. FsrA belongs to the LytTR family of proteins, which includes other virulence regulators, such as AgrA of Staphylococcus aureus, AlgR of Pseudomonas aeruginosa, and VirR of Clostridium perfringens. The LytTR DNA-binding domain that characterizes these proteins generally binds to two imperfect direct repeats separated by a number of bases that place the repeats on the same face of the DNA helix. In this study, we demonstrated that FsrA also binds to two imperfect direct repeats separated by 13 bp, based on the consensus sequence of FsrA, T/AT/CAA/GG GAA/G, which is consistent with the binding characteristics of LytTR domains. Instituto de Biotecnologia y Biologia Molecular |
description |
The FsrABDC signal transduction system is a major virulence regulator in Enterococcus faecalis. The FsrC sensor histidine kinase, upon activation by the gelatinase biosynthesis-activating pheromone (GBAP) peptide encoded by the fsrBD genes, phosphorylates the FsrA response regulator required for the transcription of the fsrBDC and the gelE-sprE genes from the fsrB promoter and the gelE promoter, respectively. FsrA belongs to the LytTR family of proteins, which includes other virulence regulators, such as AgrA of Staphylococcus aureus, AlgR of Pseudomonas aeruginosa, and VirR of Clostridium perfringens. The LytTR DNA-binding domain that characterizes these proteins generally binds to two imperfect direct repeats separated by a number of bases that place the repeats on the same face of the DNA helix. In this study, we demonstrated that FsrA also binds to two imperfect direct repeats separated by 13 bp, based on the consensus sequence of FsrA, T/AT/CAA/GG GAA/G, which is consistent with the binding characteristics of LytTR domains. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-01 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://sedici.unlp.edu.ar/handle/10915/84210 |
url |
http://sedici.unlp.edu.ar/handle/10915/84210 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/0021-9193 info:eu-repo/semantics/altIdentifier/doi/10.1128/jb.01522-10 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
eu_rights_str_mv |
openAccess |
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http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
dc.format.none.fl_str_mv |
application/pdf 1527-1532 |
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reponame:SEDICI (UNLP) instname:Universidad Nacional de La Plata instacron:UNLP |
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SEDICI (UNLP) - Universidad Nacional de La Plata |
repository.mail.fl_str_mv |
alira@sedici.unlp.edu.ar |
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13.13397 |