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Charged residues render pro-OmpA potential dependent for initiation of membrane translocation

Data up to Jan 2025

Published1993
Citations45
References44

Total Citations Per Year

Abstract

References (44)

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SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.

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A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane of Escherichia coli.

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Efficient translocation of positively charged residues of M13 procoat protein across the membrane excludes electrophoresis as the primary force for membrane insertion.

1990 • 63 citations

The cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequence.

1988 • 61 citations

Translocation of Pro-OmpA across Inner Membrane Vesicles of Escherichia coli Occurs in Two Consecutive Energetically Distinct Steps

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Recombinant forms of M13 procoat with an OmpA leader sequence or a large carboxy-terminal extension retain their independence of secY function.

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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

1991 • 29 citations

In vitro translocation of secretory proteins possessing no charges at the mature domain takes place efficiently in a protonmotive force-dependent manner.

1992 • 29 citations

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