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

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• 作者：Luisa Estrada Mallarino ; Enguo Fan ; Meike Odermatt ; Matthias M眉ller ; MeiShan Lin ; Jie Liang ; Martin Heinzelmann ; Fenja Fritsche ; Hans-J眉rgen Apell ; Wolfram Welte
• 刊名：Biochemistry
• 出版年：2015
• 出版时间：January 27, 2015
• 年：2015
• 卷：54
• 期：3
• 页码：844-852
• 全文大小：434K
• ISSN：1520-4995

文摘

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 尾-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 尾-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 尾-barrel of the Omp85 protein and augments its 尾-sheet at the first strand. Augmentation with successive 尾-strands leads to a compound, dilated barrel of both proteins.