ArticleJournal of molecular biology2012
Malleability of the folding mechanism of the outer membrane protein PagP: parallel pathways and the effect of membrane elasticity.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Sited-Directed Fluorescence Spectroscopy for Studies on the Folding and Insertion of Proteins in Lipid Bilayers and Model Membranes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Formation ofMembranes · 2023Article
- Factors That Control the Force Needed to Unfold a Membrane Protein in Silico Depend on the Mode of Denaturation.International journal of molecular sciences · 2023Article
- Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.The Journal of biological chemistry · 2020Review
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Position-Specific contribution of interface tryptophans on membrane protein energetics.Biochimica et biophysica acta. Biomembranes · 2018Article
- Outer membrane protein folding from an energy landscape perspective.BMC biology · 2017Review
- Novel Kinetic Intermediates Populated along the Folding Pathway of the Transmembrane β-Barrel OmpA.Biochemistry · 2017Article
- The safety dance: biophysics of membrane protein folding and misfolding in a cellular context.Quarterly reviews of biophysics · 2015Article
- Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase.Analytical chemistry · 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
- Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Influence of protein-micelle ratios and cysteine residues on the kinetic stability and unfolding rates of human mitochondrial VDAC-2.PloS one · 2014Article
- Sequential steps in the assembly of the multimeric outer membrane secretin PulD.The Journal of biological chemistry · 2013Article
- Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP.Journal of molecular biology · 2013Article
- Modulation of human mitochondrial voltage-dependent anion channel 2 (hVDAC-2) structural stability by cysteine-assisted barrel-lipid interactions.The Journal of biological chemistry · 2013Article
- Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel.Scientific reports · 2013Article
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4 authors.
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Abstract
Understanding the interactions between membrane proteins and the lipid bilayer is key to increasing our ability to predict and tailor the folding mechanism, structure and stability of membrane proteins. Here, we have investigated the effects of changing the membrane composition and the relative concentrations of protein and lipid on the folding mechanism of the bacterial outer membrane protein PagP. The folding pathway, monitored by tryptophan fluorescence, was found to be characterized by a burst phase, representing PagP adsorption to the liposome surface, followed by a time course that reflects the folding and insertion of the protein into the membrane. In 1,2-dilauroyl-sn-glycero-3-phosphocholine (diC(12:0)PC) liposomes, the post-adsorption time course fits well to a single exponential at high lipid-to-protein ratios (LPRs), but at low LPRs, a second exponential phase with a slower folding rate constant is observed. Interrupted refolding assays demonstrated that the two exponential phases reflect the presence of parallel folding pathways. Partitioning between these pathways was found to be modulated by the elastic properties of the membrane. Folding into mixed 1,2-dilauroyl-sn-glycero-3-phosphoethanolamine:diC(12:0)PC liposomes resulted in a decrease in PagP adsorption to the liposomes and a switch to the slower folding pathway. By contrast, inclusion of 1,2-dilauroyl-sn-glycero-3-phosphoserine into diC(12:0)PC liposomes resulted in a decrease in the folding rate of the fast pathway. The results highlight the effect of lipid composition in tailoring the folding mechanism of a membrane protein, revealing that membrane proteins have access to multiple, competing folding routes to a unique native structure.
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