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Checks and Balances in Bacterial Cell Division
Assembly of the division machinery in Gram-negative and Gram-positive bacteria occurs in two time-dependent steps. First, the FtsZ proto-ring localizes at midcell including some FtsN molecules. Subsequently, the proteins that catalyze and regulate septal peptidoglycan (PG) synthesis are recruited in...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Microbiology
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6391918/ https://www.ncbi.nlm.nih.gov/pubmed/30808703 http://dx.doi.org/10.1128/mBio.00149-19 |
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author | den Blaauwen, Tanneke Luirink, Joen |
author_facet | den Blaauwen, Tanneke Luirink, Joen |
author_sort | den Blaauwen, Tanneke |
collection | PubMed |
description | Assembly of the division machinery in Gram-negative and Gram-positive bacteria occurs in two time-dependent steps. First, the FtsZ proto-ring localizes at midcell including some FtsN molecules. Subsequently, the proteins that catalyze and regulate septal peptidoglycan (PG) synthesis are recruited including among others, the FtsBLQ-PB1B-FtsW-PBP3 complex. Further accumulation of FtsN finally allows initiation of cell division. It was known that FtsA and FtsQLB somehow prevented this initiation. Recently, A. Boes, S. Olatunji, E. Breukink, and M. Terrak (mBio 10:e01912-18, 2019, https://doi.org/10.1128/mBio.01912-18) reported that this is caused by inhibition of the activity of the PG synthases by FtsBLQ, which has to be outcompeted by accumulation of the PBP1b activating FtsN. This supports a central structural as well as regulatory role for the FtsBLQ protein complex that is conserved only in prokaryotes, making it an attractive target for antibiotic development. |
format | Online Article Text |
id | pubmed-6391918 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | American Society for Microbiology |
record_format | MEDLINE/PubMed |
spelling | pubmed-63919182019-03-04 Checks and Balances in Bacterial Cell Division den Blaauwen, Tanneke Luirink, Joen mBio Commentary Assembly of the division machinery in Gram-negative and Gram-positive bacteria occurs in two time-dependent steps. First, the FtsZ proto-ring localizes at midcell including some FtsN molecules. Subsequently, the proteins that catalyze and regulate septal peptidoglycan (PG) synthesis are recruited including among others, the FtsBLQ-PB1B-FtsW-PBP3 complex. Further accumulation of FtsN finally allows initiation of cell division. It was known that FtsA and FtsQLB somehow prevented this initiation. Recently, A. Boes, S. Olatunji, E. Breukink, and M. Terrak (mBio 10:e01912-18, 2019, https://doi.org/10.1128/mBio.01912-18) reported that this is caused by inhibition of the activity of the PG synthases by FtsBLQ, which has to be outcompeted by accumulation of the PBP1b activating FtsN. This supports a central structural as well as regulatory role for the FtsBLQ protein complex that is conserved only in prokaryotes, making it an attractive target for antibiotic development. American Society for Microbiology 2019-02-26 /pmc/articles/PMC6391918/ /pubmed/30808703 http://dx.doi.org/10.1128/mBio.00149-19 Text en Copyright © 2019 den Blaauwen and Luirink. 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 | Commentary den Blaauwen, Tanneke Luirink, Joen Checks and Balances in Bacterial Cell Division |
title | Checks and Balances in Bacterial Cell Division |
title_full | Checks and Balances in Bacterial Cell Division |
title_fullStr | Checks and Balances in Bacterial Cell Division |
title_full_unstemmed | Checks and Balances in Bacterial Cell Division |
title_short | Checks and Balances in Bacterial Cell Division |
title_sort | checks and balances in bacterial cell division |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6391918/ https://www.ncbi.nlm.nih.gov/pubmed/30808703 http://dx.doi.org/10.1128/mBio.00149-19 |
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