Impairment of twin-arginine-dependent export by seemingly small alterations of substrate conformation
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2009.07.038/fullpdf
Reference15 articles.
1. The twin-arginine translocation pathway;Panahandeh,2009
2. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli;Bolhuis;J. Biol. Chem.,2001
3. The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter;Gohlke;Proc. Natl. Acad. Sci. USA,2005
4. Functional Tat transport of unstructured, small, hydrophilic proteins;Richter;J. Biol. Chem.,2007
5. Evidence for a dynamic and transient pathway through the TAT protein transport machinery;Cline;EMBO J.,2007
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2. Engineering a Supersecreting Strain of Escherichia coli by Directed Coevolution of the Multiprotein Tat Translocation Machinery;ACS Synthetic Biology;2021-11-10
3. Engineering a super-secreting strain of Escherichia coli by directed co-evolution of the multiprotein Tat translocation machinery;2021-04-26
4. Twin-arginine translocase component TatB performs folding quality control via a general chaperone activity;2020-05-12
5. Twin-Arginine Protein Translocation;Current Topics in Microbiology and Immunology;2016
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