GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in<i> Streptococcus</i><i> pneumoniae</i> Cell Division

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A90242%2F24%3A00139177" target="_blank" >RIV/00216224:90242/24:00139177 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0022283624004194?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0022283624004194?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jmb.2024.168797" target="_blank" >10.1016/j.jmb.2024.168797</a>

Jazyk výsledku

angličtina

Název v původním jazyce

GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in<i> Streptococcus</i><i> pneumoniae</i> Cell Division

Popis výsledku v původním jazyce

StkP, the Ser/Thr protein kinase of the major human pathogen Streptococcus pneumoniae, , monitors cell wall signals and regulates growth and division in response. In vivo, , StkP interacts with GpsB, a cell division protein required for septal ring formation and closure, that affects StkP-dependent phosphorylation. Here, we report that although StkP has basal intrinsic kinase activity, GpsB promotes efficient autophosphorylation of StkP and phosphorylation of StkP substrates. Phosphoproteomic analyzes showed that GpsB is phosphorylated at several Ser and Thr residues. We confirmed that StkP directly phosphorylates GpsB in vitro and in vivo, , with T79 and T83 being the major phosphorylation sites. In vitro, , phosphoablative GpsB substitutions had a lower potential to stimulate StkP activity, whereas phosphomimetic substitutions were functional in terms of StkP activation. In vivo, , substitutions of GpsB phosphoacceptor residues, either phosphoablative or mimetic, had a negative effect on GpsB function, resulting in reduced StkP-dependent phosphorylation and impaired cell division. The bacterial two-hybrid assay and coimmunoprecipitation of GpsB from cells with differentially active StkP indicated that increased phosphorylation of GpsB resulted in a more efficient interaction of GpsB with StkP. Our data suggest that GpsB acts as an adaptor that directly promotes StkP activity by mediating interactions within the StkP signaling hub, ensuring StkP recruitment into the complex and substrate specificity. We present a model that interaction of StkP with GpsB and its phosphorylation and dephosphorylation dynamically modulate kinase activity during exponential growth and under cell wall stress of S. pneumoniae, , ensuring the proper functioning of the StkP signaling pathway. (c) 2024 The Author(s). Published by Elsevier Ltd.

Název v anglickém jazyce

GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in<i> Streptococcus</i><i> pneumoniae</i> Cell Division

Popis výsledku anglicky

StkP, the Ser/Thr protein kinase of the major human pathogen Streptococcus pneumoniae, , monitors cell wall signals and regulates growth and division in response. In vivo, , StkP interacts with GpsB, a cell division protein required for septal ring formation and closure, that affects StkP-dependent phosphorylation. Here, we report that although StkP has basal intrinsic kinase activity, GpsB promotes efficient autophosphorylation of StkP and phosphorylation of StkP substrates. Phosphoproteomic analyzes showed that GpsB is phosphorylated at several Ser and Thr residues. We confirmed that StkP directly phosphorylates GpsB in vitro and in vivo, , with T79 and T83 being the major phosphorylation sites. In vitro, , phosphoablative GpsB substitutions had a lower potential to stimulate StkP activity, whereas phosphomimetic substitutions were functional in terms of StkP activation. In vivo, , substitutions of GpsB phosphoacceptor residues, either phosphoablative or mimetic, had a negative effect on GpsB function, resulting in reduced StkP-dependent phosphorylation and impaired cell division. The bacterial two-hybrid assay and coimmunoprecipitation of GpsB from cells with differentially active StkP indicated that increased phosphorylation of GpsB resulted in a more efficient interaction of GpsB with StkP. Our data suggest that GpsB acts as an adaptor that directly promotes StkP activity by mediating interactions within the StkP signaling hub, ensuring StkP recruitment into the complex and substrate specificity. We present a model that interaction of StkP with GpsB and its phosphorylation and dephosphorylation dynamically modulate kinase activity during exponential growth and under cell wall stress of S. pneumoniae, , ensuring the proper functioning of the StkP signaling pathway. (c) 2024 The Author(s). Published by Elsevier Ltd.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

—

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Molecular Biology

ISSN

0022-2836

e-ISSN

—

Svazek periodika

436

Číslo periodika v rámci svazku

22

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

24

Strana od-do

1-24

Kód UT WoS článku

001329321900001

EID výsledku v databázi Scopus

2-s2.0-85205303128