Faculty Opinions recommendation of PASTA repeats of the protein kinase StkP interconnect cell constriction and separation of Streptococcus pneumoniae.

ABSTRACTHow bacteria control proper septum placement at midcell, to guarantee the generation of identical daughter cells, is still largely unknown. Although different systems involved in the selection of the division site have been described in selected species, these do not appear to be widely conserved. Here, we report that LocZ (Spr0334), a newly identified cell division protein, is involved in proper septum placement inStreptococcus pneumoniae. We show thatlocZis not essential but that its deletion results in cell division defects and shape deformation, causing cells to divide asymmetrically and generate unequally sized, occasionally anucleated, daughter cells. LocZ has a unique localization profile. It arrives early at midcell, before FtsZ and FtsA, and leaves the septum early, apparently moving along with the equatorial rings that mark the future division sites. Consistently, cells lacking LocZ also show misplacement of the Z-ring, suggesting that it could act as a positive regulator to determine septum placement. LocZ was identified as a substrate of the Ser/Thr protein kinase StkP, which regulates cell division in S. pneumoniae. Interestingly, homologues of LocZ are found only in streptococci, lactococci, and enterococci, indicating that this close phylogenetically related group of bacteria evolved a specific solution to spatially regulate cell division.IMPORTANCEBacterial cell division is a highly ordered process regulated in time and space. Recently, we reported that the Ser/Thr protein kinase StkP regulates cell division in Streptococcus pneumoniae, through phosphorylation of several key proteins. Here, we characterized one of the StkP substrates, Spr0334, which we named LocZ. We show that LocZ is a new cell division protein important for proper septum placement and likely functions as a marker of the cell division site. Consistently, LocZ supports proper Z-ring positioning at midcell. LocZ is conserved only among streptococci, lactococci, and enterococci, which lack homologues of the Min and nucleoid occlusion effectors, indicating that these bacteria adapted a unique mechanism to find their middle, reflecting their specific shape and symmetry.

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Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates

FEBS Journal ◽

10.1111/j.1742-4658.2005.04560.x ◽

2005 ◽

Vol 272 (5) ◽

pp. 1243-1254 ◽

Cited By ~ 88

Author(s):

Linda Nováková ◽

Lenka Sasková ◽

Petra Pallová ◽

Jiří Janeček ◽

Jana Novotná ◽

...

Keyword(s):

Streptococcus Pneumoniae ◽

Protein Kinase ◽

Protein Phosphatase ◽

Kinase Substrates

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Identification of Multiple Substrates of the StkP Ser/Thr Protein Kinase in Streptococcus pneumoniae

Journal of Bacteriology ◽

10.1128/jb.01564-09 ◽

2010 ◽

Vol 192 (14) ◽

pp. 3629-3638 ◽

Cited By ~ 49

Author(s):

Linda Nováková ◽

Silvia Bezoušková ◽

Petr Pompach ◽

Petra Špidlová ◽

Lenka Sasková ◽

...

Keyword(s):

Cell Division ◽

Streptococcus Pneumoniae ◽

Protein Kinase ◽

Intracellular Signaling ◽

Regulation Of Gene Expression ◽

Dependent Manner ◽

Α Subunit ◽

Component Systems ◽

Two Component ◽

Two Component Systems

ABSTRACT Monitoring the external environment and responding to its changes are essential for the survival of all living organisms. The transmission of extracellular signals in prokaryotes is mediated mainly by two-component systems. In addition, genomic analyses have revealed that many bacteria contain eukaryotic-type Ser/Thr protein kinases. The human pathogen Streptococcus pneumoniae encodes 13 two-component systems and has a single copy of a eukaryotic-like Ser/Thr protein kinase gene designated stkP. Previous studies demonstrated the pleiotropic role of the transmembrane protein kinase StkP in pneumococcal physiology. StkP regulates virulence, competence, and stress resistance and plays a role in the regulation of gene expression. To determine the intracellular signaling pathways controlled by StkP, we used a proteomic approach for identification of its substrates. We detected six proteins phosphorylated on threonine by StkP continuously during growth. We identified three new substrates of StkP: the Mn-dependent inorganic pyrophosphatase PpaC, the hypothetical protein spr0334, and the cell division protein DivIVA. Contrary to the results of a previous study, we did not confirm that the α-subunit of RNA polymerase is a target of StkP. We showed that StkP activation and substrate recognition depend on the presence of a peptidoglycan-binding domain comprising four extracellular penicillin-binding protein- and Ser/Thr kinase-associated domain (PASTA domain) repeats. We found that StkP is regulated in a growth-dependent manner and likely senses intracellular peptidoglycan subunits present in the cell division septa. In addition, stkP inactivation results in cell division defects. Thus, the data presented here suggest that StkP plays an important role in the regulation of cell division in pneumococcus.

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PASTA repeats of the protein kinase StkP interconnect cell constriction and separation of Streptococcus pneumoniae

Nature Microbiology ◽

10.1038/s41564-017-0069-3 ◽

2017 ◽

Vol 3 (2) ◽

pp. 197-209 ◽

Cited By ~ 23

Author(s):

Laure Zucchini ◽

Chryslène Mercy ◽

Pierre Simon Garcia ◽

Caroline Cluzel ◽

Virginie Gueguen-Chaignon ◽

...

Keyword(s):

Streptococcus Pneumoniae ◽

Protein Kinase

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Eukaryotic-Type Serine/Threonine Protein Kinase StkP Is a Global Regulator of Gene Expression in Streptococcus pneumoniae

Journal of Bacteriology ◽

10.1128/jb.01616-06 ◽

2007 ◽

Vol 189 (11) ◽

pp. 4168-4179 ◽

Cited By ~ 71

Author(s):

Lenka Sasková ◽

Linda Nováková ◽

Marek Basler ◽

Pavel Branny

Keyword(s):

Gene Expression ◽

Streptococcus Pneumoniae ◽

Protein Kinase ◽

Expression Profiles ◽

Bacterial Survival ◽

Global Regulator ◽

Cellular Processes ◽

Genes Encoding ◽

Whole Genome Expression ◽

The Impact

ABSTRACT Signal transduction pathways in both prokaryotes and eukaryotes utilize protein phosphorylation as a key regulatory mechanism. Recent studies have proven that eukaryotic-type serine/threonine protein kinases (Hank's type) are widespread in many bacteria, although little is known regarding the cellular processes they control. In this study, we have attempted to establish the role of a single eukaryotic-type protein kinase, StkP of Streptococcus pneumoniae, in bacterial survival. Our results indicate that the expression of StkP is important for the resistance of S. pneumoniae to various stress conditions. To investigate the impact of StkP on this phenotype, we compared the whole-genome expression profiles of the wild-type and ΔstkP mutant strains by microarray technology. This analysis revealed that StkP positively controls the transcription of a set of genes encoding functions involved in cell wall metabolism, pyrimidine biosynthesis, DNA repair, iron uptake, and oxidative stress response. Despite the reduced transformability of the stkP mutant, we found that the competence regulon was derepressed in the stkP mutant under conditions that normally repress natural competence development. Furthermore, the competence regulon was expressed independently of exogenous competence-stimulating peptide. In summary, our studies show that a eukaryotic-type serine/threonine protein kinase functions as a global regulator of gene expression in S. pneumoniae.

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