ArticleJournal of molecular biology2012
Structure of the phosphatase domain of the cell fate determinant SpoIIE from Bacillus subtilis.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- A single DNA methylation site regulates cell fate during Clostridioides difficile sporulation.PLoS pathogens · 2026Article
- The protein phosphatase 2C domain contributes to the pathobiological function of adenylyl cyclase inbioRxiv : the preprint server for biology · 2025Article
- Acetylation of the histone-like protein HBsu at specific sites alters gene expression during sporulation inFrontiers in microbiology · 2025Article
- Evolution and classification of Ser/Thr phosphatase PP2C family in bacteria: Sequence conservation, structures, domain distribution.PloS one · 2025Article
- Impact of nutrients on the function of the chlamydial Rsb partner switching mechanism.Pathogens and disease · 2022Article
- A Ubiquitously Conserved Cyanobacterial Protein Phosphatase Essential for High Light Tolerance in a Fast-Growing Cyanobacterium.Microbiology spectrum · 2022Article
- The FUR-like regulators PerRA and PerRB integrate a complex regulatory network that promotes mammalian host-adaptation and virulence of Leptospira interrogans.PLoS pathogens · 2021Article
- Crystal structures of the GH18 domain of the bifunctional peroxiredoxin-chitinase CotE from Clostridium difficile.Acta crystallographica. Section F, Structural biology communications · 2020Article
- SpoVG is Necessary for Sporulation inMicroorganisms · 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
- The inhibitory mechanism of aurintricarboxylic acid targeting serine/threonine phosphatase Stp1 in Staphylococcus aureus: insights from molecular dynamics simulations.Acta pharmacologica Sinica · 2019Article
- Engineering Bacillus megaterium for production of functional intracellular materials.Microbial cell factories · 2017Article
- Article
- Structure of the Branched-chain Amino Acid and GTP-sensing Global Regulator, CodY, fromThe Journal of biological chemistry · 2017Article
- Metal-dependent SpoIIE oligomerization stabilizes FtsZ during asymmetric division in Bacillus subtilis.PloS one · 2017Article
- Morphogenic Protein RodZ Interacts with Sporulation Specific SpoIIE in Bacillus subtilis.PloS one · 2016Article
- Article
- Article
- Asymmetric division and differential gene expression during a bacterial developmental program requires DivIVA.PLoS genetics · 2014Article
- Library methods for structural biology of challenging proteins and their complexes.Current opinion in structural biology · 2013Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Sporulation in Bacillus subtilis begins with an asymmetric cell division producing two genetically identical cells with different fates. SpoIIE is a membrane protein that localizes to the polar cell division sites where it causes FtsZ to relocate from mid-cell to form polar Z-rings. Following polar septation, SpoIIE establishes compartment-specific gene expression in the smaller forespore cell by dephosphorylating the anti-sigma factor antagonist SpoIIAA, leading to the release of the RNA polymerase sigma factor σ(F) from an inhibitory complex with the anti-sigma factor SpoIIAB. SpoIIE therefore couples morphological development to differential gene expression. Here, we determined the crystal structure of the phosphatase domain of SpoIIE to 2.6 Å spacing, revealing a domain-swapped dimer. SEC-MALLS (size-exclusion chromatography with multi-angle laser light scattering) analysis however suggested a monomer as the principal form in solution. A model for the monomer was derived from the domain-swapped dimer in which 2 five-stranded β-sheets are packed against one another and flanked by α-helices in an αββα arrangement reminiscent of other PP2C-type phosphatases. A flap region that controls access of substrates to the active site in other PP2C phosphatases is diminished in SpoIIE, and this observation correlates with the presence of a single manganese ion in the active site of SpoIIE in contrast to the two or three metal ions present in other PP2C enzymes. Mapping of a catalogue of mutational data onto the structure shows a clustering of sites whose point mutation interferes with the proper coupling of asymmetric septum formation to sigma factor activation and identifies a surface involved in intramolecular signaling.
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