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Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis
Membrane-anchored lipoproteins have a broad range of functions and play key roles in several cellular processes in Gram-positive bacteria. BA0330 and BA0331 are the only lipoproteins among the 11 known or putative polysaccharide deacetylases of Bacillus anthracis. We found that both lipoproteins exh...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4505593/ https://www.ncbi.nlm.nih.gov/pubmed/25825488 http://dx.doi.org/10.1074/jbc.M115.640029 |
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author | Arnaouteli, Sofia Giastas, Petros Andreou, Athina Tzanodaskalaki, Mary Aldridge, Christine Tzartos, Socrates J. Vollmer, Waldemar Eliopoulos, Elias Bouriotis, Vassilis |
author_facet | Arnaouteli, Sofia Giastas, Petros Andreou, Athina Tzanodaskalaki, Mary Aldridge, Christine Tzartos, Socrates J. Vollmer, Waldemar Eliopoulos, Elias Bouriotis, Vassilis |
author_sort | Arnaouteli, Sofia |
collection | PubMed |
description | Membrane-anchored lipoproteins have a broad range of functions and play key roles in several cellular processes in Gram-positive bacteria. BA0330 and BA0331 are the only lipoproteins among the 11 known or putative polysaccharide deacetylases of Bacillus anthracis. We found that both lipoproteins exhibit unique characteristics. BA0330 and BA0331 interact with peptidoglycan, and BA0330 is important for the adaptation of the bacterium to grow in the presence of a high concentration of salt, whereas BA0331 contributes to the maintenance of a uniform cell shape. They appear not to alter the peptidoglycan structure and do not contribute to lysozyme resistance. The high resolution x-ray structure of BA0330 revealed a C-terminal domain with the typical fold of a carbohydrate esterase 4 and an N-terminal domain unique for this family, composed of a two-layered (4 + 3) β-sandwich with structural similarity to fibronectin type 3 domains. Our data suggest that BA0330 and BA0331 have a structural role in stabilizing the cell wall of B. anthracis. |
format | Online Article Text |
id | pubmed-4505593 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | American Society for Biochemistry and Molecular Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-45055932015-07-17 Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis Arnaouteli, Sofia Giastas, Petros Andreou, Athina Tzanodaskalaki, Mary Aldridge, Christine Tzartos, Socrates J. Vollmer, Waldemar Eliopoulos, Elias Bouriotis, Vassilis J Biol Chem Microbiology Membrane-anchored lipoproteins have a broad range of functions and play key roles in several cellular processes in Gram-positive bacteria. BA0330 and BA0331 are the only lipoproteins among the 11 known or putative polysaccharide deacetylases of Bacillus anthracis. We found that both lipoproteins exhibit unique characteristics. BA0330 and BA0331 interact with peptidoglycan, and BA0330 is important for the adaptation of the bacterium to grow in the presence of a high concentration of salt, whereas BA0331 contributes to the maintenance of a uniform cell shape. They appear not to alter the peptidoglycan structure and do not contribute to lysozyme resistance. The high resolution x-ray structure of BA0330 revealed a C-terminal domain with the typical fold of a carbohydrate esterase 4 and an N-terminal domain unique for this family, composed of a two-layered (4 + 3) β-sandwich with structural similarity to fibronectin type 3 domains. Our data suggest that BA0330 and BA0331 have a structural role in stabilizing the cell wall of B. anthracis. American Society for Biochemistry and Molecular Biology 2015-05-22 2015-03-30 /pmc/articles/PMC4505593/ /pubmed/25825488 http://dx.doi.org/10.1074/jbc.M115.640029 Text en © 2015 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version free via Creative Commons CC-BY license (http://creativecommons.org/licenses/by/3.0) . |
spellingShingle | Microbiology Arnaouteli, Sofia Giastas, Petros Andreou, Athina Tzanodaskalaki, Mary Aldridge, Christine Tzartos, Socrates J. Vollmer, Waldemar Eliopoulos, Elias Bouriotis, Vassilis Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis |
title | Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis |
title_full | Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis |
title_fullStr | Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis |
title_full_unstemmed | Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis |
title_short | Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis |
title_sort | two putative polysaccharide deacetylases are required for osmotic stability and cell shape maintenance in bacillus anthracis |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4505593/ https://www.ncbi.nlm.nih.gov/pubmed/25825488 http://dx.doi.org/10.1074/jbc.M115.640029 |
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