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Literature DB >> 29165233

The Sec System: Protein Export in Escherichia coli.

Abstract

In Escherichia coli, proteins found in the periplasm or the outer membrane are exported from the cytoplasm by the general secretory, Sec, system before they acquire stably folded structure. This dynamic process involves intricate interactions among cytoplasmic and membrane proteins, both peripheral and integral, as well as lipids. In vivo, both ATP hydrolysis and proton motive force are required. Here, we review the Sec system from the inception of the field through early 2016, including biochemical, genetic, and structural data.

Entities: Chemical Species

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Year: 2017 PMID： 29165233 PMCID： PMC5807066 DOI： 10.1128/ecosalplus.ESP-0002-2017

Source DB: PubMed Journal: EcoSal Plus ISSN： 2324-6200

413 in total

The Sec System: Protein Export in Escherichia coli.

1. The ribosomal exit tunnel functions as a discriminating gate.

2. Structure of dimeric SecA, the Escherichia coli preprotein translocase motor.

3. A thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone secB.

4. Expression, purification and characterization of the Escherichia coli integral membrane protein YajC.

5. Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro.

6. A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA.

7. Effect of nonbilayer lipids on membrane binding and insertion of the catalytic domain of leader peptidase.

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

9. Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer.

10. Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase.

1. Stabilization of SecA ATPase by the primary cytoplasmic salt of Escherichia coli.

2. A Screen for Antibiotic Resistance Determinants Reveals a Fitness Cost of the Flagellum in Pseudomonas aeruginosa.

3. Substrate Proteins Take Shape at an Improved Bacterial Translocon.

4. Coassembly of SecYEG and SecA Fully Restores the Properties of the Native Translocon.

5. Investigating the stability of the SecA-SecYEG complex during protein translocation across the bacterial membrane.

6. Comparison of Single and Multiple Turnovers of SecYEG in Escherichia coli.

7. Fitness Effects of Single Amino Acid Insertions and Deletions in TEM-1 β-Lactamase.

8. Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.

Review 9. Genetic Analysis of Protein Translocation.

10. Binding of SecA ATPase monomers and dimers to lipid vesicles.