<<< Full experiment listing

PXD051731-2

PXD051731 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleGpsB coordinates StkP signalling as a PASTA kinase adaptor in Streptococcus pneumoniae cell division
DescriptionStkP, 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 in vivo. Recent phosphoproteomic analyses revealed phosphorylation of GpsB at multiple Ser and Thr residues. Here, we confirmed that StkP directly phosphorylates GpsB in vitro and in vivo, with T79 and T83 being the major phosphorylation sites. StkP has intrinsic kinase activity, but GpsB directly stimulates the autophosphorylation of StkP and phosphorylation of StkP substrates. In vitro, GpsB phosphoablative substitutions had a reduced 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, negatively affected GpsB function, resulting in reduced StkP-dependent phosphorylation and impaired cell division. Bacterial two-hybrid assay and co-immunoprecipitation 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 phosphorylation and dephosphorylation of GpsB dynamically modulate StkP activity during exponential growth and under cell wall stress of S. pneumoniae, ensuring proper functioning of the StkP signaling pathway.
HostingRepositoryPRIDE
AnnounceDate2024-09-25
AnnouncementXMLSubmission_2024-09-25_02:46:31.361.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterRudolf Kupcik
SpeciesList scientific name: Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466); NCBI TaxID: 373153;
ModificationListmethylthiolated residue; phosphorylated residue; acetylated residue
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02024-04-25 02:42:16ID requested
12024-09-25 00:56:57announced
22024-09-25 02:46:32announced2024-09-25: Updated project metadata.
Publication List
Stauberov, á V, Kube, š, a B, Joseph M, Benedet M, Furlan B, Buri, á, nkov, á K, Ulrych A, Kup, č, í, k R, Vomastek T, Massidda O, Tsui HT, Winkler ME, Branny P, Doubravov, á L, GpsB Coordinates StkP Signaling as a PASTA Kinase Adaptor in Streptococcus pneumoniae Cell Division. J Mol Biol, 436(22):168797(2024) [pubmed]
10.1016/j.jmb.2024.168797;
Keyword List
submitter keyword: phosphorylation, GpsB,Streptococcus pneumoniae
Contact List
Marie Vajrychova
contact affiliationBimedical Research Centre, University Hospital Hradec Kralove, Czech Republic
contact emailmarie.vajrychova@fnhk.cz
lab head
Rudolf Kupcik
contact affiliationBiomedical Research Centre, University Hospital Hradec Kralove, Hradec Kralove
contact emailrudolf.kupcik@fnhk.cz
dataset submitter
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/09/PXD051731
PRIDE project URI
Repository Record List
[ + ]