TtOmp85, a β-Barrel Assembly Protein, Functions by Barrel Augmentation

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2015
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Mallarino, Luisa Estrada
Fan, Enguo
Müller, Matthias
Lin, MeiShan
Liang, Jie
Heinzelmann, Martin
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Biochemistry. 2015, 54(3), pp. 844-852. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi5011305
Zusammenfassung

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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ISO 690MALLARINO, Luisa Estrada, Enguo FAN, Meike ODERMATT, Matthias MÜLLER, MeiShan LIN, Jie LIANG, Martin HEINZELMANN, Fenja FRITSCHE, Hans-Jürgen APELL, Wolfram WELTE, 2015. TtOmp85, a β-Barrel Assembly Protein, Functions by Barrel Augmentation. In: Biochemistry. 2015, 54(3), pp. 844-852. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi5011305
BibTex
@article{Mallarino2015TtOmp-31317,
  year={2015},
  doi={10.1021/bi5011305},
  title={TtOmp85, a β-Barrel Assembly Protein, Functions by Barrel Augmentation},
  number={3},
  volume={54},
  issn={0006-2960},
  journal={Biochemistry},
  pages={844--852},
  author={Mallarino, Luisa Estrada and Fan, Enguo and Odermatt, Meike and Müller, Matthias and Lin, MeiShan and Liang, Jie and Heinzelmann, Martin and Fritsche, Fenja and Apell, Hans-Jürgen and Welte, Wolfram}
}
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