The lipoprotein DolP affects cell separation in Escherichia colbut not as an upstream regulator of NlpD

Gabriela Boelter, Jack A. Bryant, Hannah Doherty, Peter Wotherspoon, Dema Alodaini, Xuyu Ma, Micheal B. Alao, Patrick J. Moynihan, Danesh Moradigaravand, Monika Glinkowska, Timothy J. Knowles, Ian R. Henderson, Manuel Banzhaf

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1 Scopus citations


Bacterial amidases are essential to split the shared envelope of adjunct daughter cells to allow cell separation. Their activity needs to be precisely controlled to prevent cell lysis. In Escherichia coli, amidase activity is controlled by three regulatory proteins NlpD, EnvC and ActS. However, recent studies linked the outer membrane lipoprotein DolP (formerly YraP) as a potential upstream regulator of NlpD. In this study we explored this link in further detail. To our surprise DolP did not modulate amidase activity in vitro and was unable to interact with NlpD in pull-down and MST (MicroScale Thermophoresis) assays. Next, we excluded the hypothesis that ΔdolP phenocopied ΔnlpD in a range of envelope stresses. However, morphological analysis of double deletion mutants of amidases (AmiA, AmiB AmiC) and amidase regulators with dolP revealed that ΔamiAΔdolP and ΔenvCΔdolP mutants display longer chain length compared to their parental strains indicating a role for DolP in cell division. Overall, we present evidence that DolP does not affect NlpD function in vitro, implying that DolP is not an upstream regulator of NlpD. However, DolP may impact daughter cell separation by interacting directly with AmiA or AmiC, or by a yet undiscovered mechanism.
Original languageEnglish (US)
JournalMicrobiology (United Kingdom)
Issue number5
StatePublished - Jan 1 2022
Externally publishedYes

Bibliographical note

Generated from Scopus record by KAUST IRTS on 2023-02-15

ASJC Scopus subject areas

  • Microbiology


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