The C Terminus of SecA Is Involved in Both Lipid Binding and SecB Binding
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Abstract
References (43)
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SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.
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Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.
1988 • 243 citations
SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.
1990 • 229 citations
Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli
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Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding.
1992 • 183 citations
SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study
1992 • 175 citations
Negatively charged phospholipids restore prePhoE translocation across phosphatidylglycerol-depleted Escherichia coli inner membranes
1991 • 159 citations
SecA protein needs both acidic phospholipids and SecY/E protein for functional high-affinity binding to the Escherichia coli plasma membrane.
1991 • 150 citations
SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer
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In vitro translocation of protein across Escherichia coli membrane vesicles requires both the proton motive force and ATP.
1987 • 130 citations
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Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region.
1990 • 115 citations
SecA, an essential component of the secretory machinery of Escherichiacoli, exists as homodimer
1991 • 108 citations
The conformation of SecA, as revealed by its protease sensitivity, is altered upon interaction with ATP, presecretory proteins, everted membrane vesicles, and phospholipids.
1991 • 100 citations
Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide
1989 • 99 citations
Construction of a lethal mutation in the synthesis of the major acidic phospholipids of Escherichia coli.
1987 • 90 citations
SecA protein autogenously represses its own translation during normal protein secretion in Escherichia coli
1989 • 74 citations
Alteration of phospholipid composition by combined defects in phosphatidylserine and cardiolipin synthases and physiological consequences in Escherichia coli
1985 • 72 citations
SecB Protein Stabilizes a Translocation-Competent State of Purified prePhoE Protein
1989 • 67 citations
OmpF-Lpp signal sequence mutants with varying charge hydrophobicity ratios provide evidence for a phosphatidylglycerol-signal sequence interaction during protein translocation across the Escherichia coli inner membrane
1993 • 61 citations
A dual role for phosphatidylglycerol in protein translocation across the Escherichia coli inner membrane.
1994 • 59 citations
Characterization of Escherichia coli SecA protein binding to a site on its mRNA involved in autoregulation.
1991 • 43 citations
Nucleotide and negatively charged lipid‐dependent vesicle aggregation caused by SecA
1993 • 33 citations
Regulation of Escherichia coli secA mRNA translation by a secretion-responsive element
1991 • 32 citations
Carboxy-Terminal Region of Escherichia coli SecA ATPase Is Important to Promote Its Protein Translocation Activity in Vivo
1994 • 29 citations
Phosphatidylglycerol dependent protein translocation across the Escherichia coli inner membrane is inhibited by the anti‐cancer drug doxorubicin
1993 • 22 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
The components of the Escherichia coli protein-transport apparatus
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