Regulation of Lytic Machineries by the FtsEX Complex in the Bacterial Divisome.
3D structure
ABC transporters
Bacterial division
Divisome
FtsE
FtsX
Lytic regulation
Mechano-transmission
PcsB
SPOR
Journal
Sub-cellular biochemistry
ISSN: 0306-0225
Titre abrégé: Subcell Biochem
Pays: United States
ID NLM: 0316571
Informations de publication
Date de publication:
2022
2022
Historique:
entrez:
23
9
2022
pubmed:
24
9
2022
medline:
28
9
2022
Statut:
ppublish
Résumé
The essential membrane complex FtsE/FtsX (FtsEX), belonging to the ABC transporter superfamily and widespread among bacteria, plays a relevant function in some crucial cell wall remodeling processes such as cell division, elongation, or sporulation. FtsEX plays a double role by recruiting proteins to the divisome apparatus and by regulating lytic activity of the cell wall hydrolases required for daughter cell separation. Interestingly, FtsEX does not act as a transporter but uses the ATPase activity of FtsE to mechanically transmit a signal from the cytosol, through the membrane, to the periplasm that activates the attached hydrolases. While the complete molecular details of such mechanism are not yet known, evidence has been recently reported that clarify essential aspects of this complex system. In this chapter we will present recent structural advances on this topic. The three-dimensional structure of FtsE, FtsX, and some of the lytic enzymes or their cognate regulators revealed an unexpected scenario in which a delicate set of intermolecular interactions, conserved among different bacterial genera, could be at the core of this regulatory mechanism providing exquisite control in both space and time of this central process to assist bacterial survival.
Identifiants
pubmed: 36151380
doi: 10.1007/978-3-031-00793-4_9
doi:
Substances chimiques
ATP-Binding Cassette Transporters
0
Bacterial Proteins
0
Cell Cycle Proteins
0
Escherichia coli Proteins
0
Adenosine Triphosphatases
EC 3.6.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
285-315Informations de copyright
© 2022. The Author(s), under exclusive license to Springer Nature Switzerland AG.
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