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SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.

Data up to Jan 2025

Published1990
Citations229
References34

Total Citations Per Year

Abstract

References (34)

DNA sequencing with chain-terminating inhibitors

1977 • 69,181 citations

Efficientin vitrosynthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter

1984 • 6,459 citations

The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers

1982 • 6,153 citations

E. coli mutant pleiotropically defective in the export of secreted proteins

1981 • 512 citations

SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.

1989 • 406 citations

Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein

1988 • 388 citations

Regulation of a membrane component required for protein secretion in escherichia coli

1982 • 356 citations

Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.

1989 • 317 citations

Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.

1988 • 243 citations

SecA protein is required for secretory protein translocation into E. coli membrane vesicles

1988 • 239 citations

A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperature-sensitive secY mutant.

1984 • 216 citations

A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins

1983 • 215 citations

Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli.

1983 • 214 citations

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

1989 • 206 citations

Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli

1988 • 188 citations

Export of Protein: A Biochemical View

1987 • 184 citations

ATP is essential for protein translocation into Escherichia coli membrane vesicles.

1985 • 163 citations

Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles.

1986 • 142 citations

ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes.

1988 • 135 citations

In vitro translocation of protein across Escherichia coli membrane vesicles requires both the proton motive force and ATP.

1987 • 130 citations

The SecY membrane component of the bacterial protein export machinery: analysis by new electrophoretic methods for integral membrane proteins.

1985 • 129 citations

Proton Motive Force-dependent and -independent Protein Translocation Revealed by an Efficient in Vitro Assay System of Escherichia coli

1989 • 107 citations

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

Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide

1989 • 99 citations

A high Concentration of SecA Allows Proton Motive Force-independent Translocation of a Model Secretory Protein into Escherichia coli Membrane Vesicles

1989 • 92 citations

Analysis of mutational alterations in the hydrophilic segment of the maltose-binding protein signal peptide

1989 • 79 citations

Role of amino-terminal positive charge on signal peptide in staphylokinase export across the cytoplasmic membrane of Escherichia coli.

1987 • 69 citations

SecA protein is directly involved in protein secretion in Escherichia coli

1989 • 68 citations

SecA suppresses the temperature-sensitive SecY24 defect in protein translocation in Escherichia coli membrane vesicles.

1988 • 62 citations

Efficient in vitro translocation into Escherichia coli membrane vesicles of a protein carrying an uncleavable signal peptide. Characterization of the translocation process.

1988 • 60 citations

Genetic Studies on Protein Export in Bacteria

1986 • 45 citations

In vitro kinetic analysis of the role of the positive charge at the amino-terminal region of signal peptides in translocation of secretory protein across the cytoplasmic membrane in Escherichia coli.

1990 • 44 citations

The role of the positively charged N-terminus of the signal sequence of E. coli outer membrane protein PhoE in export

1989 • 44 citations

Energy-dependent in vitro Translocation of a Model Protein into Escherichia Coli Inverted Membrane Vesicles Can Take Place Efficiently in the Complete Absence of the Cytosol Fraction

1989 • 17 citations

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SecA interacts with secretory proteins by recognizing the positive charge at the amino… (1990) – Journal of Biological Chemistry | Metascience Observatory Explorer