Cargando…

Topology and Organization of the Salmonella typhimurium Type III Secretion Needle Complex Components

The correct organization of single subunits of multi-protein machines in a three dimensional context is critical for their functionality. Type III secretion systems (T3SS) are molecular machines with the capacity to deliver bacterial effector proteins into host cells and are fundamental for the biol...

Descripción completa

Detalles Bibliográficos
Autores principales: Schraidt, Oliver, Lefebre, Matthew D., Brunner, Matthias J., Schmied, Wolfgang H., Schmidt, Andreas, Radics, Julia, Mechtler, Karl, Galán, Jorge E., Marlovits, Thomas C.
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848554/
https://www.ncbi.nlm.nih.gov/pubmed/20368966
http://dx.doi.org/10.1371/journal.ppat.1000824
_version_ 1782179681202601984
author Schraidt, Oliver
Lefebre, Matthew D.
Brunner, Matthias J.
Schmied, Wolfgang H.
Schmidt, Andreas
Radics, Julia
Mechtler, Karl
Galán, Jorge E.
Marlovits, Thomas C.
author_facet Schraidt, Oliver
Lefebre, Matthew D.
Brunner, Matthias J.
Schmied, Wolfgang H.
Schmidt, Andreas
Radics, Julia
Mechtler, Karl
Galán, Jorge E.
Marlovits, Thomas C.
author_sort Schraidt, Oliver
collection PubMed
description The correct organization of single subunits of multi-protein machines in a three dimensional context is critical for their functionality. Type III secretion systems (T3SS) are molecular machines with the capacity to deliver bacterial effector proteins into host cells and are fundamental for the biology of many pathogenic or symbiotic bacteria. A central component of T3SSs is the needle complex, a multiprotein structure that mediates the passage of effector proteins through the bacterial envelope. We have used cryo electron microscopy combined with bacterial genetics, site-specific labeling, mutational analysis, chemical derivatization and high-resolution mass spectrometry to generate an experimentally validated topographic map of a Salmonella typhimurium T3SS needle complex. This study provides insights into the organization of this evolutionary highly conserved nanomachinery and is the basis for further functional analysis.
format Text
id pubmed-2848554
institution National Center for Biotechnology Information
language English
publishDate 2010
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-28485542010-04-05 Topology and Organization of the Salmonella typhimurium Type III Secretion Needle Complex Components Schraidt, Oliver Lefebre, Matthew D. Brunner, Matthias J. Schmied, Wolfgang H. Schmidt, Andreas Radics, Julia Mechtler, Karl Galán, Jorge E. Marlovits, Thomas C. PLoS Pathog Research Article The correct organization of single subunits of multi-protein machines in a three dimensional context is critical for their functionality. Type III secretion systems (T3SS) are molecular machines with the capacity to deliver bacterial effector proteins into host cells and are fundamental for the biology of many pathogenic or symbiotic bacteria. A central component of T3SSs is the needle complex, a multiprotein structure that mediates the passage of effector proteins through the bacterial envelope. We have used cryo electron microscopy combined with bacterial genetics, site-specific labeling, mutational analysis, chemical derivatization and high-resolution mass spectrometry to generate an experimentally validated topographic map of a Salmonella typhimurium T3SS needle complex. This study provides insights into the organization of this evolutionary highly conserved nanomachinery and is the basis for further functional analysis. Public Library of Science 2010-04-01 /pmc/articles/PMC2848554/ /pubmed/20368966 http://dx.doi.org/10.1371/journal.ppat.1000824 Text en Schraidt et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Schraidt, Oliver
Lefebre, Matthew D.
Brunner, Matthias J.
Schmied, Wolfgang H.
Schmidt, Andreas
Radics, Julia
Mechtler, Karl
Galán, Jorge E.
Marlovits, Thomas C.
Topology and Organization of the Salmonella typhimurium Type III Secretion Needle Complex Components
title Topology and Organization of the Salmonella typhimurium Type III Secretion Needle Complex Components
title_full Topology and Organization of the Salmonella typhimurium Type III Secretion Needle Complex Components
title_fullStr Topology and Organization of the Salmonella typhimurium Type III Secretion Needle Complex Components
title_full_unstemmed Topology and Organization of the Salmonella typhimurium Type III Secretion Needle Complex Components
title_short Topology and Organization of the Salmonella typhimurium Type III Secretion Needle Complex Components
title_sort topology and organization of the salmonella typhimurium type iii secretion needle complex components
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848554/
https://www.ncbi.nlm.nih.gov/pubmed/20368966
http://dx.doi.org/10.1371/journal.ppat.1000824
work_keys_str_mv AT schraidtoliver topologyandorganizationofthesalmonellatyphimuriumtypeiiisecretionneedlecomplexcomponents
AT lefebrematthewd topologyandorganizationofthesalmonellatyphimuriumtypeiiisecretionneedlecomplexcomponents
AT brunnermatthiasj topologyandorganizationofthesalmonellatyphimuriumtypeiiisecretionneedlecomplexcomponents
AT schmiedwolfgangh topologyandorganizationofthesalmonellatyphimuriumtypeiiisecretionneedlecomplexcomponents
AT schmidtandreas topologyandorganizationofthesalmonellatyphimuriumtypeiiisecretionneedlecomplexcomponents
AT radicsjulia topologyandorganizationofthesalmonellatyphimuriumtypeiiisecretionneedlecomplexcomponents
AT mechtlerkarl topologyandorganizationofthesalmonellatyphimuriumtypeiiisecretionneedlecomplexcomponents
AT galanjorgee topologyandorganizationofthesalmonellatyphimuriumtypeiiisecretionneedlecomplexcomponents
AT marlovitsthomasc topologyandorganizationofthesalmonellatyphimuriumtypeiiisecretionneedlecomplexcomponents