@article{176586,
  keywords = {Escherichia coli, Escherichia coli Proteins, Bacterial Outer Membrane Proteins, Bacterial Outer Membrane, Gain of Function Mutation},
  author = {Elizabeth Hart and Meera Gupta and Martin W{\"u}hr and Thomas Silhavy},
  title = {The gain-of-function allele   bypasses the essential requirement for BamD in β-barrel outer membrane protein assembly},
  abstract = {<p>The outer membrane (OM) of gram-negative bacteria confers innate resistance to toxins and antibiotics. Integral β-barrel outer membrane proteins (OMPs) function to establish and maintain the selective permeability of the OM. OMPs are assembled into the OM by the β-barrel assembly machine (BAM), which is composed of one OMP-BamA-and four lipoproteins-BamB, C, D, and E. BamB, C, and E can be removed individually with only minor effects on barrier function; however, depletion of either BamA or BamD causes a global defect in OMP assembly and results in cell death. We have identified a gain-of-function mutation, , that bypasses the requirement for BamD. Although ::kan cells exhibit growth and OM barrier defects, they assemble OMPs with surprising robustness. Our results demonstrate that BamD does not play a catalytic role in OMP assembly, but rather functions to regulate the activity of BamA.</p>
},
  year = {2020},
  journal = {Proc Natl Acad Sci U S A},
  volume = {117},
  pages = {18737-18743},
  month = {08/2020},
  issn = {1091-6490},
  doi = {10.1073/pnas.2007696117},
  language = {eng},
}