The FlgT protein is involved in aeromonas hydrophila polar flagella stability and not affects anchorage of lateral flagella

Aeromonas hydrophila sodium-driven polar flagellum has a complex stator-motor. Consist of two sets of redundant and non-exchangeable proteins (PomA/PomB and PomA2/PomB2), which are homologs to other sodium-conducting polar flagellum stator motors; and also two essential proteins (MotX and MotY), tha...

Descripción completa

Detalles Bibliográficos
Autores: Merino Montero, Susana, Tomàs Magaña, Juan
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2016
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/104886
Acceso en línea:https://hdl.handle.net/2445/104886
Access Level:acceso abierto
Palabra clave:Bacteris patògens
Flagel·lats
Pathogenic bacteria
Flagellata
id ES_741a536f9d35a53ed2bb8a39d2319d21
oai_identifier_str oai:diposit.ub.edu:2445/104886
network_acronym_str ES
network_name_str España
repository_id_str
spelling The FlgT protein is involved in aeromonas hydrophila polar flagella stability and not affects anchorage of lateral flagellaMerino Montero, SusanaTomàs Magaña, JuanBacteris patògensFlagel·latsPathogenic bacteriaFlagellataAeromonas hydrophila sodium-driven polar flagellum has a complex stator-motor. Consist of two sets of redundant and non-exchangeable proteins (PomA/PomB and PomA2/PomB2), which are homologs to other sodium-conducting polar flagellum stator motors; and also two essential proteins (MotX and MotY), that they interact with one of those two redundant pairs of proteins and form the T-ring. In this work, we described an essential protein for polar flagellum stability and rotation which is orthologs to Vibrio spp. FlgT and it is encoded outside of the A. hydrophila polar flagellum regions. The flgT was present in all mesophilic Aeromonas strains tested and also in the nonmotile Aeromonas salmonicida. The A. hydrophila 1flgT mutant is able to assemble the polar flagellum but is more unstable and released into the culture supernatant from the cell upon completion assembly. Presence of FlgT in purified polar hook-basal bodies (HBB) of wild-type strain was confirmed by Western blotting and electron microscopy observations showed an outer ring of the T-ring (H-ring) which is not present in the 1flgT mutant. Anchoring and motility of proton-driven lateral flagella was not affected in the 1flgT mutant and specific antibodies did not detect FlgT in purified lateral HBB of wild type strain.Frontiers Media2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/104886Articles publicats en revistes (Genètica, Microbiologia i Estadística)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.3389/fmicb.2016.01150Frontiers in Microbiology, 2016, vol. 7, p. 1150https://doi.org/10.3389/fmicb.2016.01150cc-by (c) Merino,S. et al., 2016http://creativecommons.org/licenses/by/3.0/esinfo:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1048862026-05-27T06:46:51Z
dc.title.none.fl_str_mv The FlgT protein is involved in aeromonas hydrophila polar flagella stability and not affects anchorage of lateral flagella
title The FlgT protein is involved in aeromonas hydrophila polar flagella stability and not affects anchorage of lateral flagella
spellingShingle The FlgT protein is involved in aeromonas hydrophila polar flagella stability and not affects anchorage of lateral flagella
Merino Montero, Susana
Bacteris patògens
Flagel·lats
Pathogenic bacteria
Flagellata
title_short The FlgT protein is involved in aeromonas hydrophila polar flagella stability and not affects anchorage of lateral flagella
title_full The FlgT protein is involved in aeromonas hydrophila polar flagella stability and not affects anchorage of lateral flagella
title_fullStr The FlgT protein is involved in aeromonas hydrophila polar flagella stability and not affects anchorage of lateral flagella
title_full_unstemmed The FlgT protein is involved in aeromonas hydrophila polar flagella stability and not affects anchorage of lateral flagella
title_sort The FlgT protein is involved in aeromonas hydrophila polar flagella stability and not affects anchorage of lateral flagella
dc.creator.none.fl_str_mv Merino Montero, Susana
Tomàs Magaña, Juan
author Merino Montero, Susana
author_facet Merino Montero, Susana
Tomàs Magaña, Juan
author_role author
author2 Tomàs Magaña, Juan
author2_role author
dc.subject.none.fl_str_mv Bacteris patògens
Flagel·lats
Pathogenic bacteria
Flagellata
topic Bacteris patògens
Flagel·lats
Pathogenic bacteria
Flagellata
description Aeromonas hydrophila sodium-driven polar flagellum has a complex stator-motor. Consist of two sets of redundant and non-exchangeable proteins (PomA/PomB and PomA2/PomB2), which are homologs to other sodium-conducting polar flagellum stator motors; and also two essential proteins (MotX and MotY), that they interact with one of those two redundant pairs of proteins and form the T-ring. In this work, we described an essential protein for polar flagellum stability and rotation which is orthologs to Vibrio spp. FlgT and it is encoded outside of the A. hydrophila polar flagellum regions. The flgT was present in all mesophilic Aeromonas strains tested and also in the nonmotile Aeromonas salmonicida. The A. hydrophila 1flgT mutant is able to assemble the polar flagellum but is more unstable and released into the culture supernatant from the cell upon completion assembly. Presence of FlgT in purified polar hook-basal bodies (HBB) of wild-type strain was confirmed by Western blotting and electron microscopy observations showed an outer ring of the T-ring (H-ring) which is not present in the 1flgT mutant. Anchoring and motility of proton-driven lateral flagella was not affected in the 1flgT mutant and specific antibodies did not detect FlgT in purified lateral HBB of wild type strain.
publishDate 2016
dc.date.none.fl_str_mv 2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/104886
url https://hdl.handle.net/2445/104886
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3389/fmicb.2016.01150
Frontiers in Microbiology, 2016, vol. 7, p. 1150
https://doi.org/10.3389/fmicb.2016.01150
dc.rights.none.fl_str_mv cc-by (c) Merino,S. et al., 2016
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Merino,S. et al., 2016
http://creativecommons.org/licenses/by/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv Articles publicats en revistes (Genètica, Microbiologia i Estadística)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869410857798074368
score 15,300719

Similares en LA Referencia