ArticleThe Journal of biological chemistry2008
Evidence that the Bacillus subtilis SpoIIGA protein is a novel type of signal-transducing aspartic protease.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- Intercellular signal transduction within the mother cell compartment during Bacillus subtilis sporulation.FEMS microbiology letters · 2026Article
- Secreted retropepsin-like enzymes are essential for stress tolerance and biofilm formation inmBio · 2025Article
- SpoIIIL is a forespore factor required for efficient cell-cell signalling during Bacillus subtilis sporulation.PLoS genetics · 2025Article
- Fatty acid synthesis and utilization in gram-positive bacteria: insights fromMicrobiology and molecular biology reviews : MMBR · 2025Review
- Acetylation of the histone-like protein HBsu at specific sites alters gene expression during sporulation inFrontiers in microbiology · 2025Article
- Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024Review
- To Feed or to Stick? Genomic Analysis Offers Clues for the Role of a Molecular Machine in Endospore Formers.Journal of bacteriology · 2022Review
- Effects of DNA Topology on Transcription from rRNA Promoters inMicroorganisms · 2021Article
- Role of Regulated Proteolysis in the Communication of Bacteria With the Environment.Frontiers in molecular biosciences · 2020Review
- Diversity, versatility and complexity of bacterial gene regulation mechanisms: opportunities and drawbacks for applications in synthetic biology.FEMS microbiology reviews · 2019Review
- High-Throughput Genetic Screens Identify a Large and Diverse Collection of New Sporulation Genes in Bacillus subtilis.PLoS biology · 2016Article
- Mycobacterium tuberculosis serine protease Rv3668c can manipulate the host-pathogen interaction via Erk-NF-κB axis-mediated cytokine differential expression.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2014Article
- RC1339/APRc from Rickettsia conorii is a novel aspartic protease with properties of retropepsin-like enzymes.PLoS pathogens · 2014Article
- Spore formation in Bacillus subtilis.Environmental microbiology reports · 2014Review
- Regulated proteolysis in bacterial development.FEMS microbiology reviews · 2014Review
- Large crystal toxin formation in chromosomally engineered Bacillus thuringiensis subsp. aizawai due to σE accumulation.Applied and environmental microbiology · 2012Article
- Substrate specificity of SpoIIGA, a signal-transducing aspartic protease in Bacilli.Journal of biochemistry · 2011Article
- Loss of compartmentalization of σ(E) activity need not prevent formation of spores by Bacillus subtilis.Journal of bacteriology · 2010Article
- Hierarchical evolution of the bacterial sporulation network.Current biology : CB · 2010Review
- Pepsin homologues in bacteria.BMC genomics · 2009Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
The bacterium Bacillus subtilis undergoes endospore formation in response to starvation. sigma factors play a key role in spatiotemporal regulation of gene expression during development. Activation of sigma factors is coordinated by signal transduction between the forespore and the mother cell. sigma(E) is produced as pro-sigma(E), which is activated in the mother cell by cleavage in response to a signal from the forespore. We report that expression of SpoIIR, a putative signaling protein normally made in the forespore, and SpoIIGA, a putative protease, is necessary and sufficient for accurate, rapid, and abundant processing of pro-sigma(E) to sigma(E) in Escherichia coli. Modeling and mutational analyses provide evidence that SpoIIGA is a novel type of aspartic protease whose C-terminal half forms a dimer similar to the human immunodeficiency virus type 1 protease. Previous studies suggest that the N-terminal half of SpoIIGA is membrane-embedded. We found that SpoIIGA expressed in E. coli is membrane-associated and that after detergent treatment SpoIIGA was self-associated. Also, SpoIIGA interacts with SpoIIR. The results support a model in which SpoIIGA forms inactive dimers or oligomers, and interaction of SpoIIR with the N-terminal domain of SpoIIGA on one side of a membrane causes a conformational change that allows formation of active aspartic protease dimer in the C-terminal domain on the other side of the membrane, where it cleaves pro-sigma(E).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.