Membrane eukaryotic-like Ser/Thr protein-kinases play a pivotal role in different aspects of bacterial physiology. In contrast to the diversity of their extracellular domains, their cytoplasmic catalytic domains are highly conserved. However, the function of a long juxtamembrane domain (JMD), which connects the catalytic domain to the transmembrane helix, remains elusive. In this study, we investigated the function of the JMD of the Ser/Thr protein-kinase StkP in cell division of Streptococcus pneumoniae. We observed that the deletion of the JMD did not affect StkP kinase activity. However, it impaired the ability of StkP to phosphorylate its endogenous substrates, which resulted in significant cell morphogenesis defects. Furthermore, multiple threonine residues were identified as being phosphorylated in the JMD. To investigate the functional significance of these phosphorylation sites, we conducted an integrative analysis, combining structural biology, proteomics and bacterial cell imaging. Our results revealed that the phosphorylation of the JMD did not affect the phosphorylation of StkP substrates. However, we observed that it influenced the timing of StkP localization at the division septum and the dynamics of cell constriction. We further demonstrated that phosphorylation of the JMD facilitated the recruitment of several cell division proteins, suggesting that it is required for the assembly of the division machinery at the division septum. In conclusion, this study demonstrates that the function of the JMD of StkP is modulated by phosphorylation and critical for the cell division of S. pneumoniae. These observations may serve as a model for understanding the regulatory function of other bacterial Ser/Thr protein-kinases.
[doi:10.25345/C5N29PJ8T]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: StkP, Streptococcus pneumoniae, membrane protein-kinase, bacterial cell division, protein phosphorylation, juxtamembrane domain ; DatasetType:Proteomics
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Principal Investigators: (in alphabetical order) |
Christophe Grangeasse, MMSB-UMR5086-CNRS, France |
| Submitting User: | Adeline |
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