INVOLVEMENT OF EXPOSED POLYPEPTIDE LOOPS IN TRIMERIC STABILITY AND MEMBRANE INSERTION OF ESCHERICHIA-COLI OMPF PORIN

Different ompF-ompC gene fusions were used to analyse the regions involved in the stable trimerization and membrane insertion of the Escherichia coli OmpF porin. The stability of the trimers formed from the various hybrids was analysed. Three classes of trimer instability are observed related to the presence of different exposed polypeptide loops of OmpF. In all cases, amino acids located between residue 115 and residue 144 of OmpF are necessary to promote a correct and stable trimeric conformation. However, immunogold labelling studies indicate the correct insertion of the protein in the outer membrane despite a marked instability of some hybrid porins. The location of the residues involved in trimer stability is discussed with regards to both the three-dimensional structure and the folding of OmpF.