Cargando…

Structural Characterization of the Essential Cell Division Protein FtsE and Its Interaction with FtsX in Streptococcus pneumoniae

FtsEX is a membrane complex widely conserved across diverse bacterial genera and involved in critical processes such as recruitment of division proteins and in spatial and temporal regulation of muralytic activity during cell division or sporulation. FtsEX is a member of the ABC transporter superfam...

Descripción completa

Detalles Bibliográficos
Autores principales: Alcorlo, Martin, Straume, Daniel, Lutkenhaus, Joe, Håvarstein, Leiv Sigve, Hermoso, Juan A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Microbiology 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7468199/
https://www.ncbi.nlm.nih.gov/pubmed/32873757
http://dx.doi.org/10.1128/mBio.01488-20
_version_ 1783578167912431616
author Alcorlo, Martin
Straume, Daniel
Lutkenhaus, Joe
Håvarstein, Leiv Sigve
Hermoso, Juan A.
author_facet Alcorlo, Martin
Straume, Daniel
Lutkenhaus, Joe
Håvarstein, Leiv Sigve
Hermoso, Juan A.
author_sort Alcorlo, Martin
collection PubMed
description FtsEX is a membrane complex widely conserved across diverse bacterial genera and involved in critical processes such as recruitment of division proteins and in spatial and temporal regulation of muralytic activity during cell division or sporulation. FtsEX is a member of the ABC transporter superfamily. The component FtsX is an integral membrane protein, whereas FtsE is an ATPase and is required for the transmission of a conformational signal from the cytosol through the membrane to regulate the activity of cell wall hydrolases in the periplasm. Both proteins are essential in the major human respiratory pathogenic bacterium Streptococcus pneumoniae, and FtsX interacts with the modular peptidoglycan hydrolase PcsB at the septum. Here, we report high-resolution structures of pneumococcal FtsE bound to different nucleotides. Structural analysis revealed that FtsE contains all the conserved structural motifs associated with ATPase activity and afforded interpretation of the in vivo dimeric arrangement in both the ADP and ATP states. Interestingly, three specific FtsE regions with high structural plasticity were identified that shape the cavity in which the cytosolic region of FtsX would be inserted. The residues corresponding to the FtsX coupling helix, responsible for contacting FtsE, were identified and validated by in vivo mutagenesis studies showing that this interaction is essential for cell growth and proper morphology.
format Online
Article
Text
id pubmed-7468199
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher American Society for Microbiology
record_format MEDLINE/PubMed
spelling pubmed-74681992020-09-09 Structural Characterization of the Essential Cell Division Protein FtsE and Its Interaction with FtsX in Streptococcus pneumoniae Alcorlo, Martin Straume, Daniel Lutkenhaus, Joe Håvarstein, Leiv Sigve Hermoso, Juan A. mBio Research Article FtsEX is a membrane complex widely conserved across diverse bacterial genera and involved in critical processes such as recruitment of division proteins and in spatial and temporal regulation of muralytic activity during cell division or sporulation. FtsEX is a member of the ABC transporter superfamily. The component FtsX is an integral membrane protein, whereas FtsE is an ATPase and is required for the transmission of a conformational signal from the cytosol through the membrane to regulate the activity of cell wall hydrolases in the periplasm. Both proteins are essential in the major human respiratory pathogenic bacterium Streptococcus pneumoniae, and FtsX interacts with the modular peptidoglycan hydrolase PcsB at the septum. Here, we report high-resolution structures of pneumococcal FtsE bound to different nucleotides. Structural analysis revealed that FtsE contains all the conserved structural motifs associated with ATPase activity and afforded interpretation of the in vivo dimeric arrangement in both the ADP and ATP states. Interestingly, three specific FtsE regions with high structural plasticity were identified that shape the cavity in which the cytosolic region of FtsX would be inserted. The residues corresponding to the FtsX coupling helix, responsible for contacting FtsE, were identified and validated by in vivo mutagenesis studies showing that this interaction is essential for cell growth and proper morphology. American Society for Microbiology 2020-09-01 /pmc/articles/PMC7468199/ /pubmed/32873757 http://dx.doi.org/10.1128/mBio.01488-20 Text en Copyright © 2020 Alcorlo et al. https://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Research Article
Alcorlo, Martin
Straume, Daniel
Lutkenhaus, Joe
Håvarstein, Leiv Sigve
Hermoso, Juan A.
Structural Characterization of the Essential Cell Division Protein FtsE and Its Interaction with FtsX in Streptococcus pneumoniae
title Structural Characterization of the Essential Cell Division Protein FtsE and Its Interaction with FtsX in Streptococcus pneumoniae
title_full Structural Characterization of the Essential Cell Division Protein FtsE and Its Interaction with FtsX in Streptococcus pneumoniae
title_fullStr Structural Characterization of the Essential Cell Division Protein FtsE and Its Interaction with FtsX in Streptococcus pneumoniae
title_full_unstemmed Structural Characterization of the Essential Cell Division Protein FtsE and Its Interaction with FtsX in Streptococcus pneumoniae
title_short Structural Characterization of the Essential Cell Division Protein FtsE and Its Interaction with FtsX in Streptococcus pneumoniae
title_sort structural characterization of the essential cell division protein ftse and its interaction with ftsx in streptococcus pneumoniae
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7468199/
https://www.ncbi.nlm.nih.gov/pubmed/32873757
http://dx.doi.org/10.1128/mBio.01488-20
work_keys_str_mv AT alcorlomartin structuralcharacterizationoftheessentialcelldivisionproteinftseanditsinteractionwithftsxinstreptococcuspneumoniae
AT straumedaniel structuralcharacterizationoftheessentialcelldivisionproteinftseanditsinteractionwithftsxinstreptococcuspneumoniae
AT lutkenhausjoe structuralcharacterizationoftheessentialcelldivisionproteinftseanditsinteractionwithftsxinstreptococcuspneumoniae
AT havarsteinleivsigve structuralcharacterizationoftheessentialcelldivisionproteinftseanditsinteractionwithftsxinstreptococcuspneumoniae
AT hermosojuana structuralcharacterizationoftheessentialcelldivisionproteinftseanditsinteractionwithftsxinstreptococcuspneumoniae