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A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery
Cell elongation in rod-shaped bacteria is mediated by the Rod system, a conserved morphogenic complex that spatially controls cell wall assembly by the glycan polymerase RodA and crosslinking enzyme PBP2. Using Escherichia coli as a model system, we identified a PBP2 variant that promotes Rod system...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6207328/ https://www.ncbi.nlm.nih.gov/pubmed/30335755 http://dx.doi.org/10.1371/journal.pgen.1007726 |
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author | Rohs, Patricia D. A. Buss, Jackson Sim, Sue I. Squyres, Georgia R. Srisuknimit, Veerasak Smith, Mandy Cho, Hongbaek Sjodt, Megan Kruse, Andrew C. Garner, Ethan C. Walker, Suzanne Kahne, Daniel E. Bernhardt, Thomas G. |
author_facet | Rohs, Patricia D. A. Buss, Jackson Sim, Sue I. Squyres, Georgia R. Srisuknimit, Veerasak Smith, Mandy Cho, Hongbaek Sjodt, Megan Kruse, Andrew C. Garner, Ethan C. Walker, Suzanne Kahne, Daniel E. Bernhardt, Thomas G. |
author_sort | Rohs, Patricia D. A. |
collection | PubMed |
description | Cell elongation in rod-shaped bacteria is mediated by the Rod system, a conserved morphogenic complex that spatially controls cell wall assembly by the glycan polymerase RodA and crosslinking enzyme PBP2. Using Escherichia coli as a model system, we identified a PBP2 variant that promotes Rod system function when essential accessory components of the machinery are inactivated. This PBP2 variant hyperactivates cell wall synthesis in vivo and stimulates the activity of RodA-PBP2 complexes in vitro. Cells with the activated synthase also exhibited enhanced polymerization of the actin-like MreB component of the Rod system. Our results define an activation pathway governing Rod system function in which PBP2 conformation plays a central role in stimulating both glycan polymerization by its partner RodA and the formation of cytoskeletal filaments of MreB to orient cell wall assembly. In light of these results, previously isolated mutations that activate cytokinesis suggest that an analogous pathway may also control cell wall synthesis by the division machinery. |
format | Online Article Text |
id | pubmed-6207328 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-62073282018-11-19 A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery Rohs, Patricia D. A. Buss, Jackson Sim, Sue I. Squyres, Georgia R. Srisuknimit, Veerasak Smith, Mandy Cho, Hongbaek Sjodt, Megan Kruse, Andrew C. Garner, Ethan C. Walker, Suzanne Kahne, Daniel E. Bernhardt, Thomas G. PLoS Genet Research Article Cell elongation in rod-shaped bacteria is mediated by the Rod system, a conserved morphogenic complex that spatially controls cell wall assembly by the glycan polymerase RodA and crosslinking enzyme PBP2. Using Escherichia coli as a model system, we identified a PBP2 variant that promotes Rod system function when essential accessory components of the machinery are inactivated. This PBP2 variant hyperactivates cell wall synthesis in vivo and stimulates the activity of RodA-PBP2 complexes in vitro. Cells with the activated synthase also exhibited enhanced polymerization of the actin-like MreB component of the Rod system. Our results define an activation pathway governing Rod system function in which PBP2 conformation plays a central role in stimulating both glycan polymerization by its partner RodA and the formation of cytoskeletal filaments of MreB to orient cell wall assembly. In light of these results, previously isolated mutations that activate cytokinesis suggest that an analogous pathway may also control cell wall synthesis by the division machinery. Public Library of Science 2018-10-18 /pmc/articles/PMC6207328/ /pubmed/30335755 http://dx.doi.org/10.1371/journal.pgen.1007726 Text en © 2018 Rohs 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 (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Rohs, Patricia D. A. Buss, Jackson Sim, Sue I. Squyres, Georgia R. Srisuknimit, Veerasak Smith, Mandy Cho, Hongbaek Sjodt, Megan Kruse, Andrew C. Garner, Ethan C. Walker, Suzanne Kahne, Daniel E. Bernhardt, Thomas G. A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery |
title | A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery |
title_full | A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery |
title_fullStr | A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery |
title_full_unstemmed | A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery |
title_short | A central role for PBP2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery |
title_sort | central role for pbp2 in the activation of peptidoglycan polymerization by the bacterial cell elongation machinery |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6207328/ https://www.ncbi.nlm.nih.gov/pubmed/30335755 http://dx.doi.org/10.1371/journal.pgen.1007726 |
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