PMID: 321456Apr 10, 1977Paper

A new form of structural lipoprotein of outer membrane of Escherichia coli.

The Journal of Biological Chemistry
S HalegouaM Inouye

Abstract

Among the membrane proteins synthesized in toluene-treated cells of Escherichia coli were two distinct membrane proteins of different molecular weights, which were cross-reactive with antiserum against a structural lipoprotein of the outer membrane. One was thought to be the known membrane lipoprotein since it migrated to the same position as that of the lipoprotein (Mr = 7,200) in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. However, the other protein migrated slower than the lipoprotein. No protein corresponding to the slower-migrating species was detected in the membrane proteins synthesized in vivo. The apparent molecular weight of the protein at the new peak was estimated to be between 10,000 and 15,000. Both the new protein and the lipoprotein were found to be synthesized from stable mRNA(s) in the toluene-treated cells. The synthesis of the new protein as well as the lipoprotein was sensitive to chloramphenicol, indicating that both proteins were synthesized on ribosomes. Peptides mapping of the new protein revealed the same COOH-terminal sequence as in the lipoprotein. This indicates that the new protein has an extra sequence at the NH2-terminal end. This hypothesis is supported by the finding that the NH2...Continue Reading

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