PMID:9242980
| Citation |
Harris, F and Phoenix, DA (1997) An investigation into the ability of C-terminal homologues of Escherichia coli low molecular mass penicillin-binding proteins 4, 5 and 6 to undergo membrane interaction. Biochimie 79:171-4 |
|---|---|
| Abstract |
The Escherichia coli low molecular mass penicillin-binding proteins (PBP4, PBP5 and PBP6) are a group of penicillin-sensitive enzymes involved in the final stages of cell wall assembly. It has been suggested that these proteins may interact with the periplasmic face of the inner membrane via C-terminal amphiphilic alpha-helices. Theoretical analysis has predicted that these C-terminal helical regions may be membrane interactive. We have tested this hypothesis by assaying PBP C-terminal homologues (P4, P5 and P6) for haemolytic activity. Our results show that the PBP5 and PBP6 C-terminal homologues readily lyse sheep erythrocytes in a pH-dependent manner with LD50's of 3.5 x 10(-6) M and 6.8 x 10(-7) M respectively at pH 7. These results appear to support the present model for the membrane anchoring of PBP5 and PBP6. The PBP4 C-terminal homologue shows no evidence of haemolytic activity which could imply a different means of membrane association for PBP4. |
| Links | |
| Keywords |
Amino Acid Sequence; Animals; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Erythrocyte Membrane/metabolism; Escherichia coli/enzymology; Hemolysis/drug effects; Hexosyltransferases; Hydrogen-Ion Concentration; Melitten/pharmacology; Molecular Sequence Data; Muramoylpentapeptide Carboxypeptidase/chemistry; Muramoylpentapeptide Carboxypeptidase/metabolism; Penicillin-Binding Proteins; Peptides/chemistry; Peptides/metabolism; Peptidyl Transferases; Protein Structure, Secondary; Sheep |
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