Journal
MOLECULAR MICROBIOLOGY
Volume 90, Issue 1, Pages 88-102Publisher
WILEY
DOI: 10.1111/mmi.12348
Keywords
-
Categories
Funding
- CEA
- Agence Nationale de la Recherche [ANR-11-BSV8-005-01, ANR-12-BSV3-0008-04]
- Labex GRAL (Alliance Grenobloise pour la Biologie Structurale et Cellulaire Integrees)
- Rhone-Alpes region, Cluster Infectiologie
- Agence Nationale de la Recherche (ANR) [ANR-12-BSV3-0008] Funding Source: Agence Nationale de la Recherche (ANR)
Ask authors/readers for more resources
Bacterial cell growth and division require the co-ordinated action of peptidoglycan biosynthetic enzymes and cell morphogenesis proteins. However, the regulatory mechanisms that allow generating proper bacterial shape and thus preserving cell integrity remain largely uncharacterized, especially in ovococci. Recently, the conserved eukaryotic-like Ser/Thr protein kinase of Streptococcus pneumoniae (StkP) was demonstrated to play a major role in cell shape and division. Here, we investigate the molecular mechanisms underlying the regulatory function(s) of StkP and show that it involves one of the essential actors of septal peptidoglycan synthesis, Penicillin-Binding Protein 2x (PBP2x). We demonstrate that StkP and PBP2x interact directly and are present in the same membrane-associated complex in S.pneumoniae. We further show that they both display a late-division localization pattern at the division site and that the positioning of PBP2x depends on the presence of the extracellular PASTA domains of StkP. We demonstrate that StkP and PBP2x interaction is mediated by their extracellular regions and that the complex formation is inhibited in vitro in the presence of cell wall fragments. These data suggest that the role of StkP in cell division is modulated by an interaction with PBP2x.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available