ArticleBiochemistry2012
The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation.
Article in Biochemistry, 2012. 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, 36 citations in OpenAlex.
- The periplasmic chaperone Skp prevents misfolding of the secretory lipase A fromFrontiers in molecular biosciences · 2022Article
- Substitutions in SurA and BamA Lead to Reduced Susceptibility to Broad Range Antibiotics in Gonococci.Genes · 2021Article
- Molecular chaperones and their denaturing effect on client proteins.Journal of biomolecular NMR · 2021Article
- Affinity of Skp to OmpC revealed by single-molecule detection.Scientific reports · 2020Article
- Review
- Proteomic profiling ofBioImpacts : BI · 2020Article
- Loss of the Periplasmic Chaperone Skp and Mutations in the Efflux Pump AcrAB-TolC Play a Role in Acquired Resistance to Antimicrobial Peptides inFrontiers in microbiology · 2020Article
- Constructive approach for synthesis of a functional IgG using a reconstituted cell-free protein synthesis system.Scientific reports · 2019Article
- Distinct Contribution of the HtrA Protease and PDZ Domains to Its Function in Stress Resilience and Virulence ofFrontiers in microbiology · 2019Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- Outer membrane protein folding from an energy landscape perspective.BMC biology · 2017Review
- Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins.Scientific reports · 2016Article
- Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane Proteins.Methods in enzymology · 2016Article
- Life Stage-specific Proteomes of Legionella pneumophila Reveal a Highly Differential Abundance of Virulence-associated Dot/Icm effectors.Molecular & cellular proteomics : MCP · 2016Article
- Skp Trimer Formation Is Insensitive to Salts in the Physiological Range.Biochemistry · 2015Article
- Lipids assist the membrane insertion of a BAM-independent outer membrane protein.Scientific reports · 2015Article
- Increased Fab thermoresistance via VH-targeted directed evolution.Protein engineering, design & selection : PEDS · 2015Article
- Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?Archives of biochemistry and biophysics · 2014Review
- Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP.Journal of molecular biology · 2013Article
- Engineering Escherichia coli for soluble expression and single step purification of active human lysozyme.Journal of biotechnology · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The periplasmic seventeen kilodalton protein (Skp) chaperone has been characterized primarily for its role in outer membrane protein (OMP) biogenesis, during which the jellyfish-like trimeric protein encapsulates partially folded OMPs, protecting them from the aqueous environment until delivery to the BAM outer membrane protein insertion complex. However, Skp is increasingly recognized as a chaperone that also assists in folding soluble proteins in the bacterial periplasm. In this capacity, Skp coexpression increases the active yields of many recombinant proteins and bacterial virulence factors. Using a panel of single-chain antibodies and a single-chain T-cell receptor (collectively termed scFvs) possessing varying stabilities and biophysical characteristics, we performed in vivo expression and in vitro folding and aggregation assays in the presence or absence of Skp. For Skp-sensitive scFvs, the presence of Skp during in vitro refolding assays reduced aggregation but did not alter the observed folding rates, resulting in a higher overall yield of active protein. Of the proteins analyzed, Skp sensitivity in all assays correlated with the presence of folding intermediates, as observed with urea denaturation studies. These results are consistent with Skp acting as a holdase, sequestering partially folded intermediates and thereby preventing aggregation. Because not all soluble proteins are sensitive to Skp coexpression, we hypothesize that the presence of a long-lived protein folding intermediate renders a protein sensitive to Skp. Improved understanding of the bacterial periplasmic protein folding machinery may assist in high-level recombinant protein expression and may help identify novel approaches to block bacterial virulence.
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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.