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Research Papers

The first 28 amino acids of mature LamB are required for rapid and efficient export from the cytoplasm.

Department of Molecular Biology, Lewis Thomas Laboratory, Princeton University, NJ 08544.

Abstract

Our laboratory has been utilizing the Escherichia coli outer membrane protein LamB to study the mechanism of protein localization. Various lines of evidence suggest that, in addition to a signal sequence, regions within the mature protein are required for efficient localization. In particular, studies using LamB-LacZ hybrid proteins have identified regions between amino acids 27 and 49 of mature LamB, which may play an important role in localization. To elucidate further the function of these regions, a series of in-frame deletions that remove varying lengths of early lamB sequences was constructed. The effects of these deletions on export of a large LamB-LacZ hybrid protein, 42-1, and on export of an otherwise wild-type LamB protein were determined. We find a strong correlation between the sequences deleted and the export phenotypes these deletions impart to both LamB and the LamB-LacZ42-1 hybrid protein. On the basis of these findings, the deletions can be divided into several distinct classes that define a region within mature LamB that participates in localization. This region extends amino terminally from amino acid 28 of the mature protein and functions in the rapid and efficient localization of LamB from the cytoplasm.

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