ArticleJournal of bacteriology2004
Two outer membrane proteins are required for maximal type I secretion of the Caulobacter crescentus S-layer protein.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Cell cycle dependent coordination of surface layer biogenesis in Caulobacter crescentus.Nature communications · 2024Article
- Engineering High-Yield Biopolymer Secretion Creates an Extracellular Protein Matrix for Living Materials.mSystems · 2021Article
- Topologically-guided continuous protein crystallization controls bacterial surface layer self-assembly.Nature communications · 2019Article
- Engineering the S-Layer of Caulobacter crescentus as a Foundation for Stable, High-Density, 2D Living Materials.ACS synthetic biology · 2019Article
- Generation of a Dual-Target, Safe, Inexpensive Microbicide that Protects Against HIV-1 and HSV-2 Disease.Scientific reports · 2018Article
- Environmental Calcium Controls Alternate Physical States of the Caulobacter Surface Layer.Biophysical journal · 2017Article
- Two Outer Membrane Proteins Contribute to Caulobacter crescentus Cellular Fitness by Preventing Intracellular S-Layer Protein Accumulation.Applied and environmental microbiology · 2016Article
- ATP-binding Cassette (ABC) Transport System Solute-binding Protein-guided Identification of Novel d-Altritol and Galactitol Catabolic Pathways in Agrobacterium tumefaciens C58.The Journal of biological chemistry · 2015Article
- Transposon Mutagenesis Paired with Deep Sequencing of Caulobacter crescentus under Uranium Stress Reveals Genes Essential for Detoxification and Stress Tolerance.Journal of bacteriology · 2015Article
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- Proteome variation among Filifactor alocis strains.Proteomics · 2012Article
- An essential tyrosine phosphatase homolog regulates cell separation, outer membrane integrity, and morphology in Caulobacter crescentus.Journal of bacteriology · 2011Article
- RTX proteins: a highly diverse family secreted by a common mechanism.FEMS microbiology reviews · 2010Review
- The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane {beta}-barrel proteins in Caulobacter crescentus.Microbiology (Reading, England) · 2010Article
- S-layer-mediated display of the immunoglobulin G-binding domain of streptococcal protein G on the surface of Caulobacter crescentus: development of an immunoactive reagent.Applied and environmental microbiology · 2007Article
- S-layer anchoring and localization of an S-layer-associated protease in Caulobacter crescentus.Journal of bacteriology · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transport of RsaA, the crystalline S-layer subunit protein of Caulobacter crescentus, is mediated by a type I secretion mechanism. Two proteins have been identified that play the role of the outer membrane protein (OMP) component in the RsaA secretion machinery. The genes rsaF(a) and rsaF(b) were identified by similarity to the Escherichia coli hemolysin secretion OMP TolC by using the C. crescentus genome sequence. The rsaF(a) gene is located several kilobases downstream of the other transporter genes, while rsaF(b) is completely unlinked. An rsaF(a) knockout had approximately 56% secretion compared to wild-type levels, while the rsaF(b) knockout reduced secretion levels to approximately 79%. When expression of both proteins was eliminated, there was no RsaA secretion, but a residual level of approximately 9% remained inside the cell, suggesting posttranslational autoregulation. Complementation with either of the individual rsaF genes by use of a multicopy vector, which resulted in 8- to 10-fold overexpression of the proteins, did not restore RsaA secretion to wild-type levels, indicating that both rsaF genes were required for full-level secretion. However, overexpression of rsaF(a) (with normal rsaF(b) levels) in concert with overexpression of rsaA resulted in a 28% increase in RsaA secretion, indicating a potential for significantly increasing expression levels of an already highly expressing type I secretion system. This is the only known example of type I secretion requiring two OMPs to assemble a fully functional system.
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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.