Cargando…
Penicillin-binding protein redundancy in Bacillus subtilis enables growth during alkaline shock
Penicillin-binding proteins (PBPs) play critical roles in cell wall construction, cell shape, and bacterial replication. Bacteria maintain a diversity of PBPs, indicating that despite their apparent functional redundancy, there is differentiation across the PBP family. Seemingly redundant proteins c...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10055284/ https://www.ncbi.nlm.nih.gov/pubmed/36993441 http://dx.doi.org/10.1101/2023.03.20.533529 |
_version_ | 1785015849225027584 |
---|---|
author | Mitchell, Stephanie L. Kearns, Daniel B. Carlson, Erin E. |
author_facet | Mitchell, Stephanie L. Kearns, Daniel B. Carlson, Erin E. |
author_sort | Mitchell, Stephanie L. |
collection | PubMed |
description | Penicillin-binding proteins (PBPs) play critical roles in cell wall construction, cell shape, and bacterial replication. Bacteria maintain a diversity of PBPs, indicating that despite their apparent functional redundancy, there is differentiation across the PBP family. Seemingly redundant proteins can be important for enabling an organism to cope with environmental stressors. We sought to evaluate the consequence of environmental pH on PBP enzymatic activity in Bacillus subtilis. Our data show that a subset of B. subtilis PBPs change activity levels during alkaline shock and that one PBP isoform is rapidly modified to generate a smaller protein (i.e., PBP1a to PBP1b). Our results indicate that a subset of the PBPs are preferred for growth under alkaline conditions, while others are readily dispensable. Indeed, we found that this phenomenon could also be observed in Streptococcus pneumoniae, implying that it may be generalizable across additional bacterial species and further emphasizing the evolutionary benefit of maintaining many, seemingly redundant periplasmic enzymes. |
format | Online Article Text |
id | pubmed-10055284 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Cold Spring Harbor Laboratory |
record_format | MEDLINE/PubMed |
spelling | pubmed-100552842023-03-30 Penicillin-binding protein redundancy in Bacillus subtilis enables growth during alkaline shock Mitchell, Stephanie L. Kearns, Daniel B. Carlson, Erin E. bioRxiv Article Penicillin-binding proteins (PBPs) play critical roles in cell wall construction, cell shape, and bacterial replication. Bacteria maintain a diversity of PBPs, indicating that despite their apparent functional redundancy, there is differentiation across the PBP family. Seemingly redundant proteins can be important for enabling an organism to cope with environmental stressors. We sought to evaluate the consequence of environmental pH on PBP enzymatic activity in Bacillus subtilis. Our data show that a subset of B. subtilis PBPs change activity levels during alkaline shock and that one PBP isoform is rapidly modified to generate a smaller protein (i.e., PBP1a to PBP1b). Our results indicate that a subset of the PBPs are preferred for growth under alkaline conditions, while others are readily dispensable. Indeed, we found that this phenomenon could also be observed in Streptococcus pneumoniae, implying that it may be generalizable across additional bacterial species and further emphasizing the evolutionary benefit of maintaining many, seemingly redundant periplasmic enzymes. Cold Spring Harbor Laboratory 2023-03-20 /pmc/articles/PMC10055284/ /pubmed/36993441 http://dx.doi.org/10.1101/2023.03.20.533529 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator. |
spellingShingle | Article Mitchell, Stephanie L. Kearns, Daniel B. Carlson, Erin E. Penicillin-binding protein redundancy in Bacillus subtilis enables growth during alkaline shock |
title | Penicillin-binding protein redundancy in Bacillus subtilis enables growth during alkaline shock |
title_full | Penicillin-binding protein redundancy in Bacillus subtilis enables growth during alkaline shock |
title_fullStr | Penicillin-binding protein redundancy in Bacillus subtilis enables growth during alkaline shock |
title_full_unstemmed | Penicillin-binding protein redundancy in Bacillus subtilis enables growth during alkaline shock |
title_short | Penicillin-binding protein redundancy in Bacillus subtilis enables growth during alkaline shock |
title_sort | penicillin-binding protein redundancy in bacillus subtilis enables growth during alkaline shock |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10055284/ https://www.ncbi.nlm.nih.gov/pubmed/36993441 http://dx.doi.org/10.1101/2023.03.20.533529 |
work_keys_str_mv | AT mitchellstephaniel penicillinbindingproteinredundancyinbacillussubtilisenablesgrowthduringalkalineshock AT kearnsdanielb penicillinbindingproteinredundancyinbacillussubtilisenablesgrowthduringalkalineshock AT carlsonerine penicillinbindingproteinredundancyinbacillussubtilisenablesgrowthduringalkalineshock |