ArticleJournal of bacteriology1999
Temporal expression of the Bacillus subtilis secA gene, encoding a central component of the preprotein translocase.
Article in Journal of bacteriology, 1999. 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.
- Stop codon reassignment to tryptophan in members of the bacterial phylumMicrobial genomics · 2026Article
- Microbial membrane transport genes in maize rhizosphere under fertilization - a preliminary study.Scientific reports · 2026Article
- Recombinant production of acidophilic L-arabinose isomerase from Lentilactobacillus parakefiri in Bacillus subtilis.Microbial cell factories · 2025Article
- Protein secretion zones during overexpression of amylase within the Gram-positive cell wall.BMC biology · 2023Article
- Article
- Construction of a High-Expression System in Bacillus through Transcriptomic Profiling and Promoter Engineering.Microorganisms · 2020Article
- Promoter engineering enables overproduction of foreign proteins from a single copy expression cassette in Bacillus subtilis.Microbial cell factories · 2019Article
- Proteases HtrA and HtrB for α-amylase secreted from Bacillus subtilis in secretion stress.Cell stress & chaperones · 2019Review
- Factors Influencing Recombinant Protein Secretion Efficiency in Gram-Positive Bacteria: Signal Peptide and Beyond.Frontiers in bioengineering and biotechnology · 2019Article
- Signal peptides for recombinant protein secretion in bacterial expression systems.Microbial cell factories · 2018Review
- Bottleneck in secretion of α-amylase in Bacillus subtilis.Microbial cell factories · 2017Review
- Differential expression of secretion machinery during bacterial growth: SecY and SecF decrease while SecA increases during transition from exponential phase to stationary phase.Current microbiology · 2013Article
- Live-cell imaging tool optimization to study gene expression levels and dynamics in single cells of Bacillus cereus.Applied and environmental microbiology · 2013Article
- Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels.Biochemical and biophysical research communications · 2013Article
- Enhanced extracellular production of heterologous proteins in Bacillus subtilis by deleting the C-terminal region of the SecA secretory machinery.Molecular biotechnology · 2010Article
- Production and secretion stress caused by overexpression of heterologous alpha-amylase leads to inhibition of sporulation and a prolonged motile phase in Bacillus subtilis.Applied and environmental microbiology · 2007Article
- Comparative proteomic analysis of high cell density cultivations with two recombinant Bacillus megaterium strains for the production of a heterologous dextransucrase.Proteome science · 2006Article
- Mapping the pathways to staphylococcal pathogenesis by comparative secretomics.Microbiology and molecular biology reviews : MMBR · 2006Review
- Quantitation of the capacity of the secretion apparatus and requirement for PrsA in growth and secretion of alpha-amylase in Bacillus subtilis.Journal of bacteriology · 2001Article
- Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome.Microbiology and molecular biology reviews : MMBR · 2000Review
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Authors and funding
5 authors.
Funding
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Abstract
In Bacillus subtilis, the secretion of extracellular proteins strongly increases upon transition from exponential growth to the stationary growth phase. It is not known whether the amounts of some or all components of the protein translocation apparatus are concomitantly increased in relation to the increased export activity. In this study, we analyzed the transcriptional organization and temporal expression of the secA gene, encoding a central component of the B. subtilis preprotein translocase. We found that secA and the downstream gene (prfB) constitute an operon that is transcribed from a vegetative (sigmaA-dependent) promoter located upstream of secA. Furthermore, using different independent methods, we found that secA expression occurred mainly in the exponential growth phase, reaching a maximal value almost precisely at the transition from exponential growth to the stationary growth phase. Following to this maximum, the de novo transcription of secA sharply decreased to a low basal level. Since at the time of maximal secA transcription the secretion activity of B. subtilis strongly increases, our results clearly demonstrate that the expression of at least one of the central components of the B. subtilis protein export apparatus is adapted to the increased demand for protein secretion. Possible mechanistic consequences are discussed.
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