Separate Analysis of Twin-arginine Translocation (Tat)-specific Membrane Binding and Translocation in Escherichia coli
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference30 articles.
1. Protein traffic in bacteria: Multiple routes from the ribosome to and across the membrane
2. Protein targeting by the twin-arginine translocation pathway
3. The Tat protein export pathway
4. A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli
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1. Length matters: Functional flip of the short TatA transmembrane helix;Biophysical Journal;2022-12
2. Envelope Stress Activates Expression of the Twin Arginine Translocation (Tat) System in Salmonella;Microbiology Spectrum;2022-10-26
3. Interplay between MPIase, YidC, and PMF during Sec-independent insertion of membrane proteins;Life Science Alliance;2021-10-12
4. Ring assembly of c subunits of F 0 F 1 ‐ATP synthase in Propionigenium modestum requires YidC and UncI following MPIase‐dependent membrane insertion;FEBS Letters;2021-01-29
5. Twin-arginine translocation (Tat) mutants in Salmonella enterica serovar Typhimurium have increased susceptibility to cell wall targeting antibiotics;FEMS Microbes;2021
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