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Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD

The nonessential process of peptidoglycan synthesis during Bacillus subtilis sporulation is one model to study bacterial cell wall biogenesis. SpoVD is a class B high-molecular-weight penicillin-binding protein that is specific for sporulation. Strains lacking this protein produce spores without the...

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Autores principales: Bukowska-Faniband, Ewa, Hederstedt, Lars
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Blackwell Publishing Ltd 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3906833/
https://www.ncbi.nlm.nih.gov/pubmed/23789716
http://dx.doi.org/10.1111/1574-6968.12202
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author Bukowska-Faniband, Ewa
Hederstedt, Lars
author_facet Bukowska-Faniband, Ewa
Hederstedt, Lars
author_sort Bukowska-Faniband, Ewa
collection PubMed
description The nonessential process of peptidoglycan synthesis during Bacillus subtilis sporulation is one model to study bacterial cell wall biogenesis. SpoVD is a class B high-molecular-weight penicillin-binding protein that is specific for sporulation. Strains lacking this protein produce spores without the peptidoglycan cortex layer and are heat sensitive. The detailed functions of the four different protein domains of SpoVD are unknown, and the observed phenotype of strains lacking the entire protein could be an indirect defect. We therefore inactivated the transpeptidase domain by substitution of the active-site serine residue. Our results demonstrate that endospore cortex synthesis depends on the transpeptidase activity of SpoVD specifically.
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spelling pubmed-39068332014-02-03 Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD Bukowska-Faniband, Ewa Hederstedt, Lars FEMS Microbiol Lett Research Letters The nonessential process of peptidoglycan synthesis during Bacillus subtilis sporulation is one model to study bacterial cell wall biogenesis. SpoVD is a class B high-molecular-weight penicillin-binding protein that is specific for sporulation. Strains lacking this protein produce spores without the peptidoglycan cortex layer and are heat sensitive. The detailed functions of the four different protein domains of SpoVD are unknown, and the observed phenotype of strains lacking the entire protein could be an indirect defect. We therefore inactivated the transpeptidase domain by substitution of the active-site serine residue. Our results demonstrate that endospore cortex synthesis depends on the transpeptidase activity of SpoVD specifically. Blackwell Publishing Ltd 2013-09 2013-07-08 /pmc/articles/PMC3906833/ /pubmed/23789716 http://dx.doi.org/10.1111/1574-6968.12202 Text en Federation of European Microbiological Societies Published by John Wiley & Sons Ltd. All rights reserved http://creativecommons.org/licenses/by/3.0/ This is an open access article under the terms of the Creative Commons Attribution–NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
spellingShingle Research Letters
Bukowska-Faniband, Ewa
Hederstedt, Lars
Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD
title Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD
title_full Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD
title_fullStr Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD
title_full_unstemmed Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD
title_short Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD
title_sort cortex synthesis during bacillus subtilis sporulation depends on the transpeptidase activity of spovd
topic Research Letters
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3906833/
https://www.ncbi.nlm.nih.gov/pubmed/23789716
http://dx.doi.org/10.1111/1574-6968.12202
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