Abstract
Abstract We discuss the utility of MalF as a model system for the study of protein assembly into the cytoplasmic membrane of Escherichia coli . Our studies have demonstrated the importance of various sequences within MalF for membrane insertion and topology. The sequences that play the preeminent role in determining topology are the positively charged hydrophilic cytoplasmic domains. The position of these domains relative to hydrophobic membrane spanning segments (MSS) determines which MSS act as protein export signals and which act as stop-transfer sequences. Using alkaline phosphatase fusions, we have shown that both the cytoplasmic domains and the membrane spanning segments vary in the strength with which they promote proper topology. The process of membrane insertion of the MalF protein is independent of the normal secretion apparatus for protein export in E. coli . Finally, the influence of the other membrane components of the maltose transport complex, MalG and MalK, on MalF assembly is examined. While these proteins have no detectable effect on either the membrane insertion or topology of MalF, they do influence the final structure that MalF assumes in the membrane.
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