ArticleBiochemistry2015
TtOmp85, a β-barrel assembly protein, functions by barrel augmentation.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs.Scientific reports · 2024Article
- Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding.Communications biology · 2022Article
- Large-Scale Conformational Changes of FhaC Provide Insights Into the Two-Partner Secretion Mechanism.Frontiers in molecular biosciences · 2022Article
- Inward-facing glycine residues create sharp turns in β-barrel membrane proteins.Biochimica et biophysica acta. Biomembranes · 2021Article
- Outer membrane permeability: Antimicrobials and diverse nutrients bypass porins inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Interplay of protein primary sequence, lipid membrane, and chaperone in β-barrel assembly.Protein science : a publication of the Protein Society · 2021Article
- The Principles of Protein Targeting and Transport Across Cell Membranes.The protein journal · 2019Review
- Molecular basis for the folding of β-helical autotransporter passenger domains.Nature communications · 2018Article
- Membrane protein insertion through a mitochondrial β-barrel gate.Science (New York, N.Y.) · 2018Article
- Engineering a Novel Porin OmpGF Via Strand Replacement from Computational Analysis of Sequence Motif.Biochimica et biophysica acta. Biomembranes · 2017Article
- A tamB homolog is involved in maintenance of cell envelope integrity and stress resistance of Deinococcus radiodurans.Scientific reports · 2017Article
- The β-barrel assembly machinery in motion.Nature reviews. Microbiology · 2017Review
- Skp is a multivalent chaperone of outer-membrane proteins.Nature structural & molecular biology · 2016Article
- Lipids assist the membrane insertion of a BAM-independent outer membrane protein.Scientific reports · 2015Article
- Evolution of the Translocation and Assembly Module (TAM).Genome biology and evolution · 2015Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Outer membrane proteins are vital for Gram-negative bacteria and organisms that inherited organelles from them. Proteins from the Omp85/BamA family conduct the insertion of membrane proteins into the outer membrane. We show that an eight-stranded outer membrane β-barrel protein, TtoA, is inserted and folded into liposomes by an Omp85 homologue. Furthermore, we recorded the channel conductance of this Omp85 protein in black lipid membranes, alone and in the presence of peptides comprising the sequence of the two N-terminal and the two C-terminal β-strands of TtoA. Only with the latter could a long-living compound channel that exhibits conductance levels higher than those of the Omp85 protein alone be observed. These data support a model in which unfolded outer membrane protein after docking with its C-terminus penetrates into the transmembrane β-barrel of the Omp85 protein and augments its β-sheet at the first strand. Augmentation with successive β-strands leads to a compound, dilated barrel of both proteins.
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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.