ArticlePloS one2017
Metal-dependent SpoIIE oligomerization stabilizes FtsZ during asymmetric division in Bacillus subtilis.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Evolution and classification of Ser/Thr phosphatase PP2C family in bacteria: Sequence conservation, structures, domain distribution.PloS one · 2025Article
- Cell division machinery drives cell-specific gene activation during differentiation inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- PAS domain containing regulator SLCG_7083 involved in morphological development and glucose utilization in Streptomyces lincolnensis.Microbial cell factories · 2023Article
- Sporulation in solventogenic and acetogenic clostridia.Applied microbiology and biotechnology · 2021Review
- Linking the Peptidoglycan Synthesis Protein Complex with Asymmetric Cell Division duringInternational journal of molecular sciences · 2020Article
- Single-molecule optical microscopy of protein dynamics and computational analysis of images to determine cell structure development in differentiatingComputational and structural biotechnology journal · 2020Article
- Purification and characterization of FtsZ from the citrus canker pathogen Xanthomonas citri subsp. citri.MicrobiologyOpen · 2019Article
- A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity.The Journal of biological chemistry · 2018Article
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Authors and funding
4 authors.
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Abstract
SpoIIE is a bifunctional protein involved in asymmetric septum formation and in activation of the forespore compartment-specific transcription factor σF through dephosphorylation of SpoIIAA-P. The phosphatase activity of SpoIIE requires Mn2+ as a metal cofactor. Here, we show that the presence of a metal cofactor also influences SpoIIE oligomerization and asymmetric septum formation. Absence of Mn2+ from sporulation medium results in a delay of the formation of polar FtsZ-rings, similar to a spoIIE null mutant. We purified the entire cytoplasmic part of the SpoIIE protein, and show that the protein copurifies with bound metals. Metal binding both stimulates SpoIIE oligomerization, and results in the formation of larger oligomeric structures. The presence of SpoIIE oligomers reduces FtsZ GTP hydrolysis activity and stabilizes FtsZ polymers in a light scattering assay. Combined, these results indicate that metal binding is not just required for SpoIIE phosphatase activity but also is important for SpoIIE's role in asymmetric septum formation.
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