PXD032931

PXD032931 is an original dataset announced via ProteomeXchange.

Title	PrkA regulates Bacillus subtilis sporulation through a Lon protease activity
Description	In Bacillus subtilis, sporulation is a sequential and highly regulated process. Phosphorylation events by Histidine or Serine/Threonine kinases are key points in this regulation. PrkA has been proposed to be an essential Serine kinase for the initiation of sporulation but its kinase activity has not been clearly demonstrated so far. Indeed, neither its autophosphorylation nor identification of a B. subtilis phosphorylated substrate was unambiguously established. Bioinformatic homology searches revealed sequence similarities with the AAA+ ATP-dependent Lon protease family. Here, we showed that PrkA is indeed able to hydrolyse the α-casein, an exogenous substrate of Lon proteases, in an ATP-dependent manner. We also showed that this ATP-dependent protease activity is essential for PrkA function in sporulation since mutation in the Walker A motif leads to a sporulation defect. Furthermore, we found that PrkA protease activity is tightly regulated by phosphorylation events involving one of the Ser/Thr kinases of B. subtilis, PrkC, as characterized by mass spectrometry from 3 in vitro independent experiments (1: PrkA+PrkC/2:PrKA-S219E+PrkC/3: PrKA-T217E+PrkC). We finally demonstrated that PrkA regulation of the transcriptional factor σK via the transition phase regulator ScoC is certainly indirect.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:25:41.392.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Regine Lebrun
SpeciesList	scientific name: Bacillus subtilis subsp. subtilis str. 168; NCBI TaxID: 224308;
ModificationList	phosphorylated residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2022-04-02 13:27:46	ID requested
1	2022-10-14 19:48:26	announced
⏵ 2	2023-11-14 08:25:44	announced	2023-11-14: Updated project metadata.

Zhang A, Lebrun R, Espinosa L, Galinier A, Pompeo F, PrkA is an ATP-dependent protease that regulates sporulation in Bacillus subtilis. J Biol Chem, 298(10):102436(2022) [pubmed]

submitter keyword: ATPase, PrkA,Lon protease, sporulation, phosphorylation, Bacillus subtilis

Régine Lebru
contact affiliation	Aix-Marseille Univ, CNRS, FR3479, Proteomics facility of Institut de Microbilogie de la Méditerranée, Marseille Protéomique
contact email	rlebrun@imm.cnrs.fr
lab head
Regine Lebrun
contact affiliation	CNRS
contact email	rlebrun@imm.cnrs.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD032931
     1. Label: PRIDE project
     2. Name: PrkA regulates Bacillus subtilis sporulation through a Lon protease activity