Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan; Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki, Japan
Nakajohn Thewasano
Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan; Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki, Japan
Kenichiro Imai
Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tokyo, Japan
Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan; Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki, Japan
Rebecca S Bamert
Centre to Impact AMR, Monash University, Clayton, Australia; Infection Program, Biomedicine Discovery Institute, and Department of Microbiology, Monash University, Clayton, Australia
Centre to Impact AMR, Monash University, Clayton, Australia; Infection Program, Biomedicine Discovery Institute, and Department of Microbiology, Monash University, Clayton, Australia
Rhys A Dunstan
Centre to Impact AMR, Monash University, Clayton, Australia; Infection Program, Biomedicine Discovery Institute, and Department of Microbiology, Monash University, Clayton, Australia
Yue Ding
Department of Materials Science and Engineering, Monash University, Clayton, Australia; Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
Yukari Nakajima
Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan; Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki, Japan
XiangFeng Lai
Department of Materials Science and Engineering, Monash University, Clayton, Australia
Chaille T Webb
Centre to Impact AMR, Monash University, Clayton, Australia; Infection Program, Biomedicine Discovery Institute, and Department of Microbiology, Monash University, Clayton, Australia
Kentaro Hidaka
Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan; Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki, Japan
Kher Shing Tan
Centre to Impact AMR, Monash University, Clayton, Australia; Infection Program, Biomedicine Discovery Institute, and Department of Microbiology, Monash University, Clayton, Australia
Department of Materials Science and Engineering, Monash University, Clayton, Australia; Biomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Clayton, Australia
Trevor Lithgow
Centre to Impact AMR, Monash University, Clayton, Australia; Infection Program, Biomedicine Discovery Institute, and Department of Microbiology, Monash University, Clayton, Australia
Frontier Science Research Center, University of Miyazaki, Miyazaki, Japan; Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki, Japan
Outer membrane proteins (OMPs) are essential components of the outer membrane of Gram-negative bacteria. In terms of protein targeting and assembly, the current dogma holds that a ‘β-signal’ imprinted in the final β-strand of the OMP engages the β-barrel assembly machinery (BAM) complex to initiate membrane insertion and assembly of the OMP into the outer membrane. Here, we revealed an additional rule that signals equivalent to the β-signal are repeated in other, internal β-strands within bacterial OMPs, by peptidomimetic and mutational analysis. The internal signal is needed to promote the efficiency of the assembly reaction of these OMPs. BamD, an essential subunit of the BAM complex, recognizes the internal signal and the β-signal, arranging several β-strands and partial folding for rapid OMP assembly. The internal signal-BamD ordering system is not essential for bacterial viability but is necessary to retain the integrity of the outer membrane against antibiotics and other environmental insults.
