ArticleJournal of bacteriology2001
Quantitation of the capacity of the secretion apparatus and requirement for PrsA in growth and secretion of alpha-amylase in Bacillus subtilis.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 100 citations in OpenAlex.
- Divergent contributions of multiple PPIases to cell survival, sociality, and stress tolerance inApplied and environmental microbiology · 2026Article
- Overcoming cellular secretion bottlenecks: advanced secretion engineering and molecular tailoring for next-generation microbial α-amylases with enhanced industrial performance.World journal of microbiology & biotechnology · 2026Review
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- The chaperone PrsA2 regulates the secretion, stability, and folding of listeriolysin O duringmBio · 2024Article
- The Construction of an Environmentally Friendly Super-Secreting Strain ofInternational journal of molecular sciences · 2024Article
- Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A.BMC microbiology · 2024Article
- Automation-aided construction and characterization ofFrontiers in bioengineering and biotechnology · 2024Article
- Protein secretion zones during overexpression of amylase within the Gram-positive cell wall.BMC biology · 2023Article
- CRISPRi screen for enhancing heterologous α-amylase yield in Bacillus subtilis.Journal of industrial microbiology & biotechnology · 2023Article
- The impact of PrsA over-expression on theFrontiers in microbiology · 2022Article
- Redirected Stress Responses in a Genome-Minimized 'midimSystems · 2021Article
- Deletion of a Peptidylprolyl Isomerase Gene Results in the Inability ofApplied and environmental microbiology · 2020Article
- Functional identification of aOpen biology · 2019Article
- Identification and optimization of PrsA in Bacillus subtilis for improved yield of amylase.Microbial cell factories · 2019Article
- Enhanced extracellular expression of Bacillus stearothermophilus α-amylase in Bacillus subtilis through signal peptide optimization, chaperone overexpression and α-amylase mutant selection.Microbial cell factories · 2019Article
- Bottleneck in secretion of α-amylase in Bacillus subtilis.Microbial cell factories · 2017Review
- A structural comparison of Listeria monocytogenes protein chaperones PrsA1 and PrsA2 reveals molecular features required for virulence.Molecular microbiology · 2016Article
- The Staphylococcus aureus Chaperone PrsA Is a New Auxiliary Factor of Oxacillin Resistance Affecting Penicillin-Binding Protein 2A.Antimicrobial agents and chemotherapy · 2015Article
- Combinatorial Sec pathway analysis for improved heterologous protein secretion in Bacillus subtilis: identification of bottlenecks by systematic gene overexpression.Microbial cell factories · 2015Article
- Dimeric Structure of the Bacterial Extracellular Foldase PrsA.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Regulated expression of AmyQ alpha-amylase of Bacillus amyloliquefaciens was used to examine the capacity of the protein secretion apparatus of B. subtilis. One B. subtilis cell was found to secrete maximally 10 fg of AmyQ per h. The signal peptidase SipT limits the rate of processing of the signal peptide. Another limit is set by PrsA lipoprotein. The wild-type level of PrsA was found to be 2 x 10(4) molecules per cell. Decreasing the cellular level of PrsA did not decrease the capacity of the protein translocation or signal peptide processing steps but dramatically affected secretion in a posttranslocational step. There was a linear correlation between the number of cellular PrsA molecules and the number of secreted AmyQ molecules over a wide range of prsA and amyQ expression levels. Significantly, even when amyQ was expressed at low levels, overproduction of PrsA enhanced its secretion. The finding is consistent with a reversible interaction between PrsA and AmyQ. The high cellular level of PrsA suggests a chaperone-like function. PrsA was also found to be essential for the viability of B. subtilis. Drastic depletion of PrsA resulted in altered cellular morphology and ultimately in cell death.
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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.