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Deciphering the Role of a SLOG Superfamily Protein YpsA in Gram-Positive Bacteria
Bacteria adapt to different environments by regulating cell division and several conditions that modulate cell division have been documented. Understanding how bacteria transduce environmental signals to control cell division is critical in understanding the global network of cell division regulatio...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6459960/ https://www.ncbi.nlm.nih.gov/pubmed/31024470 http://dx.doi.org/10.3389/fmicb.2019.00623 |
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author | Brzozowski, Robert S. Huber, Mirella Burroughs, A. Maxwell Graham, Gianni Walker, Merryck Alva, Sameeksha S. Aravind, L. Eswara, Prahathees J. |
author_facet | Brzozowski, Robert S. Huber, Mirella Burroughs, A. Maxwell Graham, Gianni Walker, Merryck Alva, Sameeksha S. Aravind, L. Eswara, Prahathees J. |
author_sort | Brzozowski, Robert S. |
collection | PubMed |
description | Bacteria adapt to different environments by regulating cell division and several conditions that modulate cell division have been documented. Understanding how bacteria transduce environmental signals to control cell division is critical in understanding the global network of cell division regulation. In this article we describe a role for Bacillus subtilis YpsA, an uncharacterized protein of the SLOG superfamily of nucleotide and ligand-binding proteins, in cell division. We observed that YpsA provides protection against oxidative stress as cells lacking ypsA show increased susceptibility to hydrogen peroxide treatment. We found that the increased expression of ypsA leads to filamentation and disruption of the assembly of FtsZ, the tubulin-like essential protein that marks the sites of cell division in B. subtilis. We also showed that YpsA-mediated filamentation is linked to the growth rate. Using site-directed mutagenesis, we targeted several conserved residues and generated YpsA variants that are no longer able to inhibit cell division. Finally, we show that the role of YpsA is possibly conserved in Firmicutes, as overproduction of YpsA in Staphylococcus aureus also impairs cell division. |
format | Online Article Text |
id | pubmed-6459960 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-64599602019-04-25 Deciphering the Role of a SLOG Superfamily Protein YpsA in Gram-Positive Bacteria Brzozowski, Robert S. Huber, Mirella Burroughs, A. Maxwell Graham, Gianni Walker, Merryck Alva, Sameeksha S. Aravind, L. Eswara, Prahathees J. Front Microbiol Microbiology Bacteria adapt to different environments by regulating cell division and several conditions that modulate cell division have been documented. Understanding how bacteria transduce environmental signals to control cell division is critical in understanding the global network of cell division regulation. In this article we describe a role for Bacillus subtilis YpsA, an uncharacterized protein of the SLOG superfamily of nucleotide and ligand-binding proteins, in cell division. We observed that YpsA provides protection against oxidative stress as cells lacking ypsA show increased susceptibility to hydrogen peroxide treatment. We found that the increased expression of ypsA leads to filamentation and disruption of the assembly of FtsZ, the tubulin-like essential protein that marks the sites of cell division in B. subtilis. We also showed that YpsA-mediated filamentation is linked to the growth rate. Using site-directed mutagenesis, we targeted several conserved residues and generated YpsA variants that are no longer able to inhibit cell division. Finally, we show that the role of YpsA is possibly conserved in Firmicutes, as overproduction of YpsA in Staphylococcus aureus also impairs cell division. Frontiers Media S.A. 2019-04-05 /pmc/articles/PMC6459960/ /pubmed/31024470 http://dx.doi.org/10.3389/fmicb.2019.00623 Text en Copyright © 2019 Brzozowski, Huber, Burroughs, Graham, Walker, Alva, Aravind and Eswara. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Brzozowski, Robert S. Huber, Mirella Burroughs, A. Maxwell Graham, Gianni Walker, Merryck Alva, Sameeksha S. Aravind, L. Eswara, Prahathees J. Deciphering the Role of a SLOG Superfamily Protein YpsA in Gram-Positive Bacteria |
title | Deciphering the Role of a SLOG Superfamily Protein YpsA in Gram-Positive Bacteria |
title_full | Deciphering the Role of a SLOG Superfamily Protein YpsA in Gram-Positive Bacteria |
title_fullStr | Deciphering the Role of a SLOG Superfamily Protein YpsA in Gram-Positive Bacteria |
title_full_unstemmed | Deciphering the Role of a SLOG Superfamily Protein YpsA in Gram-Positive Bacteria |
title_short | Deciphering the Role of a SLOG Superfamily Protein YpsA in Gram-Positive Bacteria |
title_sort | deciphering the role of a slog superfamily protein ypsa in gram-positive bacteria |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6459960/ https://www.ncbi.nlm.nih.gov/pubmed/31024470 http://dx.doi.org/10.3389/fmicb.2019.00623 |
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