Glycine-144 is required for efficient folding of outer membrane protein PhoE of Escherichia coli K12

H de Cock, N Quaedvlieg, D Bosch, M Scholten, J Tommassen

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Short stretches of similar sequences have been detected in unrelated bacterial outer membrane proteins (Nikaido and Wu (1984) Proc. Natl. Acad. Sci. USA 81, 1048-1052). In the most pronounced similarity region, only a glycine residue is absolutely conserved. To investigate whether this glycine residue is essential for outer membrane incorporation, oligonucleotide-directed mutagenesis was applied to replace this residue, i.e. Gly-144, as well as two other Gly-residues in pore protein PhoE. Substitution of Gly-52 and Gly-258 by Ala and Val, respectively, did not influence outer membrane incorporation. However, the substitution of Gly-144 by Leu affected the efficiency of outer membrane incorporation. After in vitro synthesis this mutant protein was less efficiently precipitated with monoclonal antibodies that recognize conformational epitopes than wild-type PhoE, showing that the mutation interferes with correct folding of the protein.

Original languageEnglish
Pages (from-to)285-8
Number of pages4
JournalFEBS Letters
Issue number2
Publication statusPublished - 25 Feb 1991


  • Bacterial Outer Membrane Proteins
  • DNA Mutational Analysis
  • Escherichia coli
  • Glycine
  • Macromolecular Substances
  • Porins
  • Precipitin Tests
  • Recombinant Proteins
  • Structure-Activity Relationship


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