ArticleFrontiers in microbiology2015
Heat shock proteins IbpA and IbpB are required for NlpI-participated cell division in Escherichia coli.
Article in Frontiers in microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Determination of the genome-scale metabolic network ofFrontiers in bioengineering and biotechnology · 2025Article
- Structural basis for recruitment of peptidoglycan endopeptidase MepS by lipoprotein NlpI.Nature communications · 2024Article
- Comparative Genomics of an Emerging Multidrug-ResistantAntibiotics (Basel, Switzerland) · 2024Article
- L-Arabinose Transport and Metabolism inFrontiers in cellular and infection microbiology · 2021Article
- Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates.PLoS genetics · 2019Article
- Human Gut Microbiota: Toward an Ecology of Disease.Frontiers in microbiology · 2017Review
- Acetylation of Lysine 201 Inhibits the DNA-Binding Ability of PhoP to Regulate Salmonella Virulence.PLoS pathogens · 2016Article
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Authors and funding
7 authors.
Funding
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Abstract
Lipoprotein NlpI of Escherichia coli is involved in the cell division, virulence, and bacterial interaction with eukaryotic host cells. To elucidate the functional mechanism of NlpI, we examined how NlpI affects cell division and found that induction of NlpI inhibits nucleoid division and halts cell growth. Consistent with these results, the cell division protein FtsZ failed to localize at the septum but diffused in the cytosol. Elevation of NlpI expression enhanced the transcription and the outer membrane localization of the heat shock protein IbpA and IbpB. Deletion of either ibpA or ibpB abolished the effects of NlpI induction, which could be restored by complementation. The C-terminus of NlpI is critical for the enhancement in IbpA and IbpB production, and the N-terminus of NlpI is required for the outer membrane localization of NlpI, IbpA, and IbpB. Furthermore, NlpI physically interacts with IbpB. These results indicate that over-expression of NlpI can interrupt the nucleoids division and the assembly of FtsZ at the septum, mediated by IbpA/IbpB, suggesting a role of the NlpI/IbpA/IbpB complex in the cell division.
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