Molecular basis of the final step of cell division in Streptococcus pneumoniae.
CP: Microbiology
LytB
SAXS
StkP
Streptococcus pneumoniae
bacterial division
cell wall
crystallography
molecular dynamics
peptidoglycan
teichoic acid
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
25 07 2023
25 07 2023
Historique:
received:
02
02
2023
revised:
13
05
2023
accepted:
21
06
2023
medline:
31
7
2023
pubmed:
7
7
2023
entrez:
7
7
2023
Statut:
ppublish
Résumé
Bacterial cell-wall hydrolases must be tightly regulated during bacterial cell division to prevent aberrant cell lysis and to allow final separation of viable daughter cells. In a multidisciplinary work, we disclose the molecular dialogue between the cell-wall hydrolase LytB, wall teichoic acids, and the eukaryotic-like protein kinase StkP in Streptococcus pneumoniae. After characterizing the peptidoglycan recognition mode by the catalytic domain of LytB, we further demonstrate that LytB possesses a modular organization allowing the specific binding to wall teichoic acids and to the protein kinase StkP. Structural and cellular studies notably reveal that the temporal and spatial localization of LytB is governed by the interaction between specific modules of LytB and the final PASTA domain of StkP. Our data collectively provide a comprehensive understanding of how LytB performs final separation of daughter cells and highlights the regulatory role of eukaryotic-like kinases on lytic machineries in the last step of cell division in streptococci.
Identifiants
pubmed: 37418323
pii: S2211-1247(23)00767-2
doi: 10.1016/j.celrep.2023.112756
pmc: PMC10434722
mid: NIHMS1920496
pii:
doi:
Substances chimiques
Protein Serine-Threonine Kinases
EC 2.7.11.1
Teichoic Acids
0
Bacterial Proteins
0
Protein Kinases
EC 2.7.-
Hydrolases
EC 3.-
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
112756Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM131685
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI131685
Pays : United States
Informations de copyright
Copyright © 2023 The Author(s). Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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