Penicillin-binding protein redundancy in

Bacillus activity-based probes cell division pH regulation penicillin-binding proteins

Journal

bioRxiv : the preprint server for biology
Titre abrégé: bioRxiv
Pays: United States
ID NLM: 101680187

Informations de publication

Date de publication:
20 Mar 2023
Historique:
pubmed: 31 3 2023
medline: 31 3 2023
entrez: 30 3 2023
Statut: epublish

Résumé

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

Identifiants

pubmed: 36993441
doi: 10.1101/2023.03.20.533529
pmc: PMC10055284
pii:
doi:

Types de publication

Preprint

Langues

eng

Déclaration de conflit d'intérêts

Conflicts of Interest The authors declare that they have no conflicts of interest with the contents of this article.

Auteurs

Stephanie L Mitchell (SL)

Department of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455.

Daniel B Kearns (DB)

Department of Biology, Indiana University, Bloomington, Indiana 47405.

Erin E Carlson (EE)

Department of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455.
Departments of Medicinal Chemistry, Biochemistry, Molecular Biology and Biophysics, and Pharmacology, University of Minnesota, Minneapolis, Minnesota 55455.

Classifications MeSH