Proper insertion of a complex membrane protein in the absence of its amino-terminal export signal
In: Journal of Biological Chemistry, Jg. 266 (1991) ; Nr. 25, S. 16530-16533
Zeitschriftenaufsatz / Fach: Biologie
ehem. Fakultät für Biologie und Geografie
The MalF protein spans the Escherichia coli cytoplasmic membrane eight times. Deletion of the first transmembrane stretch of MalF, which acts as an export signal, results in a truncated protein that still exhibits high levels of maltose transport activity. These and additional results indicate that the orientation of a membrane protein is not determined by the amino-terminal export signal, topological information is distributed throughout the MalF protein, and insertion of a protein into the cytoplasmic membrane can occur nonsequentially.