Lysozyme-promoted association of protein I molecules in the outer membrane of Escherichia coli.
Incubation of whole envelopes prepared from sonically oscillated Escherichia coli K-12 cultures with lysozyme in vitro resulted in the appearance of a protein species with an apparent molecular weight double that of outer membrane protein I. Similar dimers were also detected in purified outer membranes and whole envelopes from lysozyme-induced spheroplasts of E. coli K-12. This was confirmed by two-dimensional electrophoresis in which the dimers were resolved in the second dimension to run as single polypeptides of protein I. Formation of dimers was correlated with peptidoglycan degradation, but the ability of protein I molecules to associate may vary between strains of E. coli, since dimers were found only in outer membranes from E. coli W7. We suggest that extensive degradation of peptidoglycan leads to nonspecific formation of protein I aggregates, but that these aggregates do not occur in vivo.
D001426:Bacterial Proteins / Q000032:analysis; D002473:Cell Wall / Q000378:metabolism / Q000648:ultrastructure; D004926:Escherichia coli / Q000378:metabolism / Q000648:ultrastructure*; D008970:Molecular Weight; D009113:Muramidase / Q000378:metabolism*; D010455:Peptides / Q000032:analysis; D010457:Peptidoglycan / Q000378:metabolism; D013104:Spheroplasts / Q000648:ultrastructure
D001426:Bacterial Proteins; D010455:Peptides; D010457:Peptidoglycan; D009113:Muramidase