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Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes

Data up to Jan 2025

Published1993
Citations70
References34

Total Citations Per Year

Abstract

References (34)

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Positively charged residues are important determinants of membrane protein topology

1990 • 132 citations

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Introduction of basic amino acid residues after the signal peptide inhibits protein translocation across the cytoplasmic membrane of Escherichia coli. Relation to the orientation of membrane proteins.

1988 • 100 citations

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

1991 • 95 citations

A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coli.

1987 • 90 citations

Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteins

1984 • 84 citations

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The role of the polar, carboxyl-terminal domain of Escherichia coli leader peptidase in its translocation across the plasma membrane.

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

1988 • 61 citations

Export incompatibility of N-terminal basic residues in a mature polypeptide of Eschericbia coli can be alleviated by optimising the signal peptide

1990 • 55 citations

Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal.

1989 • 48 citations

The internal signal sequence of Escherichia coli leader peptidase is necessary, but not sufficient, for its rapid membrane assembly.

1987 • 47 citations

Both a short hydrophobic domain and a carboxyl-terminal hydrophilic region are important for signal function in the Escherichia coli leader peptidase

1989 • 30 citations

Characterization of the internal signal-anchor domain of Escherichia coli leader peptidase.

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Alteration of N-terminal residues of mature human lysozyme affects its secretion in yeast and translocation into canine microsomal vesicles.

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Deleted Work

1955 • 0 citations

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