Real-time monitoring of peptidoglycan synthesis by membrane-reconstituted penicillin-binding proteins.
E. coli
Förster Resonance Energy Transfer
assay
bacterial cell wall
biochemistry
chemical biology
penicillin-binding protein
peptidoglycan
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
24 02 2021
24 02 2021
Historique:
received:
28
07
2020
accepted:
23
02
2021
pubmed:
25
2
2021
medline:
29
1
2022
entrez:
24
2
2021
Statut:
epublish
Résumé
Peptidoglycan is an essential component of the bacterial cell envelope that surrounds the cytoplasmic membrane to protect the cell from osmotic lysis. Important antibiotics such as β-lactams and glycopeptides target peptidoglycan biosynthesis. Class A penicillin-binding proteins (PBPs) are bifunctional membrane-bound peptidoglycan synthases that polymerize glycan chains and connect adjacent stem peptides by transpeptidation. How these enzymes work in their physiological membrane environment is poorly understood. Here, we developed a novel Förster resonance energy transfer-based assay to follow in real time both reactions of class A PBPs reconstituted in liposomes or supported lipid bilayers and applied this assay with PBP1B homologues from
Identifiants
pubmed: 33625355
doi: 10.7554/eLife.61525
pii: 61525
pmc: PMC7943195
doi:
pii:
Substances chimiques
Escherichia coli Proteins
0
Penicillin-Binding Proteins
0
Peptidoglycan
0
Peptidoglycan Glycosyltransferase
EC 2.4.1.129
penicillin-binding protein 1B, E coli
EC 2.4.1.129
Serine-Type D-Ala-D-Ala Carboxypeptidase
EC 3.4.16.4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : BBSRC
ID : BB/R017409/1
Informations de copyright
© 2021, Hernández-Rocamora et al.
Déclaration de conflit d'intérêts
VH, NB, KP, EB, ML, WV No competing interests declared
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