title: TtOmp85, a β-barrel assembly protein, functions by barrel augmentation.
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.
authors.affiliation: Department of Biology, University of Konstanz , Universitätsstraße 10, 78457 Konstanz, Germany.
authors.forename: Luisa
authors.initials: L
authors.lastname: Estrada Mallarino
authors.forename: Enguo
authors.initials: E
authors.lastname: Fan
authors.forename: Meike
authors.initials: M
authors.lastname: Odermatt
authors.forename: Matthias
authors.initials: M
authors.lastname: Müller
authors.forename: MeiShan
authors.initials: M
authors.lastname: Lin
authors.forename: Jie
authors.initials: J
authors.lastname: Liang
authors.forename: Martin
authors.initials: M
authors.lastname: Heinzelmann
authors.forename: Fenja
authors.initials: F
authors.lastname: Fritsche
authors.forename: Hans-Jürgen
authors.initials: HJ
authors.lastname: Apell
authors.forename: Wolfram
authors.initials: W
authors.lastname: Welte
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D015640:Ion Channel Gating; D008958:Models, Molecular; D010455:Peptides / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011510:Proteolipids / Q000378:metabolism; D013816:Thermodynamics; D016963:Thermus thermophilus / Q000378:metabolism*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D010455:Peptides; D011510:Proteolipids; C020485:proteoliposomes