Proteomics

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Pull-down of polyP chains and associated proteins with PPBD as a bait

ABSTRACT: CobB interacts polyP in E. coli stressed cells. The goal of the performed experiment was to identify proteins interacting polyP in E. coli cells encountering amino acid starvation. We used Co-NTA resin with immobilized PPBD for capturing and isolation of polyP, together with bound proteins. The MS analysis followed by a Mascot search against the E. coli database revealed 98 proteins identified (based on ≥ 3 peptides) in the extract prepared from wild-type E. coli MG1655 grown for 3 hours in MOPS. It must be pointed out that we obtained high background in the control lysate prepared from Δppk mutant, however in a comparative analysis, 21 proteins were qualified as interesting candidates that bind polyP in the tested conditions. Among them, CobB deacetylase was identified.

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli Bacteria

SUBMITTER: Paulina Czaplewska  

LAB HEAD: Paulina Czaplewska

PROVIDER: PXD062171 | Pride | 2026-03-02

REPOSITORIES: Pride

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Publications

PolyP inhibits CobB deacetylase triggering a regulatory coupling to prevent DNA replication initiation.

Boguszewska Ewelina E   Hirsz Zuzanna Z   Sroka Magdalena M   Bury Katarzyna K   Chmura Weronika W   Strzałka Agnieszka A   Kołodziej Marta M   Zakrzewska-Czerwińska Jolanta J   Konieczny Igor I  

Nucleic acids research 20260201 4

Polyphosphate (polyP) is considered having regulatory functions in both procaryotic and eucaryotic cells. Under certain stress conditions, bacteria accumulate polyP, which results in liquid-liquid phase separation and polyP granules formation with not fully uncovered functions. We demonstrate that in starved Escherichia coli cells, replication initiator DnaA protein fails to form defined foci and does not bind to the origin of DNA replication (oriC), while to some extent interacts other sites on  ...[more]

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