Chapter 3 Molecular characterization of Sec proteins comprising the protein secretory machinery of Escherichia coli

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• Publication year

  1992

• Venue

  New Comprehensive Biochemistry

• Publication date

  Unknown publication date

• Fields of study

  Biology, Chemistry

• Identifiers
  DOI 10.1016/S0167-7306(08)60080-0
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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

  1992cited by this paper
• The requirement of a positive charge at the amino terminus can be compensated for by a longer central hydrophobic stretch in the functioning of signal peptides.

  1992cited by this paper
• SecY, SecE, and band 1 form the membrane-embedded domain of Escherichia coli preprotein translocase.

  1992cited by this paper
• Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli.

  1991cited by this paper
• The primary pathway of protein export in E. coli.

  1991cited by this paper
• Negatively charged phospholipids restore prePhoE translocation across phosphatidylglycerol-depleted Escherichia coli inner membranes.

  1991cited by this paper
• A bacterium catches up

  1991cited by this paper
• 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.

  1991cited by this paper
• Purification of SecE and reconstitution of SecE‐dependent protein translocation activity

  1991cited by this paper
• The conformation of SecA, as revealed by its protease sensitivity, is altered upon interaction with ATP, presecretory proteins, everted membrane vesicles, and phospholipids.

  1991cited by this paper
• In vitro biochemical studies on translocation of presecretory proteins across the cytoplasmic membrane of Escherichia coli.

  1991cited by this paper
• ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase

  1991cited by this paper
• One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.

  1991cited by this paper
• The enzymology of protein translocation across the Escherichia coli plasma membrane.

  1991cited by this paper
• SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer.

  1991cited by this paper
• Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli.

  1991cited by this paper
• SecY is an indispensable component of the protein secretory machinery of Escherichia coli.

  1991cited by this paper
• Proton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coli translocase.

  1991cited by this paper
• Quantitative renaturation from a guanidine-denatured state of the SecA dimer, a 200 KDa protein involved in protein secretion in Escherichia coli.

  1990cited by this paper
• The secD locus of E.coli codes for two membrane proteins required for protein export.

  1990cited by this paper
• Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region.

  1990cited by this paper
• The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane.

  1990cited by this paper
• SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.

  1990cited by this paper
• PrlA (SecY) and PrlG (SecE) interact directly and function sequentially during protein translocation in E. coli.

  1990cited by this paper
• Assembly of translocation-competent proteoliposomes from detergent-solubilized rough microsomes.

  1990cited by this paper
• SecE‐dependent overproduction of SecY in Escherichia coli

  1990cited by this paper
• SecB protein: A cytosolic export factor that associates with nascent exported proteins

  1990cited by this paper
• The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins.

  1990cited by this paper
• The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

  1990cited by this paper
• Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization.

  1990cited by this paper
• SecY protein, a membrane-embedded secretion factor of E. coli, is cleaved by the ompT protease in vitro.

  1990cited by this paper
• Thesec andprl genes ofEscherichia coli

  1990cited by this paper
• Signal peptidases and signal peptide hydrolases

  1990cited by this paper
• Proton motive force-dependent and -independent protein translocation revealed by an efficient in vitro assay system of Escherichia coli.

  1989cited by this paper
• The secE gene encodes an integral membrane protein required for protein export in Escherichia coli.

  1989cited by this paper
• SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.

  1989cited by this paper
• Specific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli.

  1989cited by this paper
• Translocation of pro-OmpA across inner membrane vesicles of Escherichia coli occurs in two consecutive energetically distinct steps.

  1989cited by this paper
• In vitro analysis of the process of translocation of OmpA across the Escherichia coli cytoplasmic membrane. A translocation intermediate accumulates transiently in the absence of the proton motive force.

  1989cited by this paper
• SecA protein is directly involved in protein secretion in Escherichia coli

  1989cited by this paper
• SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.

  1989cited by this paper
• Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.

  1988cited by this paper
• SecA protein is required for secretory protein translocation into E. coli membrane vesicles.

  1988cited by this paper
• Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli

  1988cited by this paper
• SecA suppresses the temperature-sensitive SecY24 defect in protein translocation in Escherichia coli membrane vesicles.

  1988cited by this paper
• Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli.

  1987cited by this paper
• Overproduction, isolation and determination of the amino-terminal sequence of the SecY protein, a membrane protein involved in protein export in Escherichia coli.

  1986cited by this paper
• Overproduction of Escherichia coli replication proteins by the use of runaway-replication plasmids

  1983cited by this paper
• Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation.

  1983cited by this paper
• Mechanism of export of outer membrane lipoproteins through the cytoplasmic membrane in Escherichia coli. Binding of lipoprotein precursors to the peptidoglycan layer.

  1982cited by this paper
• Regulation of a membrane component required for protein secretion in Escherichia coli.

  1982cited by this paper
• E. coli mutant pleiotropically defective in the export of secreted proteins.

  1981cited by this paper

• SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels

  2018cites this paper
• Biphasic actions of SecA inhibitors on Prl/Sec suppressors: Possible physiological roles of SecA-only channels.

  2017cites this paper
• Quantitation of the Capacity of the Secretion Apparatus and Requirement for PrsA in Growth and Secretion of α-Amylase inBacillus subtilis

  2001cites this paper
• Bacillus subtilis in-Amylase α PrsA in Growth and Secretion of Secretion Apparatus and Requirement for Quantitation of the Capacity of the

  2001cites this paper
• Beta-galactosidase is inactivated by intermolecular disulfide bonds and is toxic when secreted to the periplasm of Escherichia coli

  1995cites this paper
• Biochemical analyses of components comprising the protein translocation machinery of Escherichia coli

  1995cites this paper
• Biochemical characterization of the presecretory protein translocation machinery of Escherichia coli

  1994cites this paper