Charged residues render pro-OmpA potential dependent for initiation of membrane translocation
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References (44)
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The cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequence.
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Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal.
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A proline residue near the amino terminus of the mature domain of secretory proteins lowers the level of the proton motive force required for translocation
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In vitro translocation of secretory proteins possessing no charges at the mature domain takes place efficiently in a protonmotive force-dependent manner.
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