Evidence for interactions between domains of TatA and TatB from mutagenesis of the TatABC subunits of the twin-arginine translocase
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2005.04654.x/fullpdf
Reference40 articles.
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2. Evolutionarily related insertion pathways of bacterial, mitochondrial, and thylakoid membrane proteins;Dalbey;Annu Rev Cell Dev Biol,2000
3. A folded protein can be transported across the chloroplast envelope and thylakoid membranes;Clark;Mol Biol Cell,1997
4. The Sec-independent twin-arginine translocation system can transport both tightly folded and malfolded proteins across the thylakoid membrane;Hynds;J Biol Chem,1998
5. A common export pathway for proteins binding complex redox cofactors?;Berks;Mol Microbiol,1996
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1. Assembling the Tat protein translocase;eLife;2016-12-03
2. Twin-arginine translocation-arresting protein regions contact TatA and TatB;Biological Chemistry;2014-07-01
3. Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways;Research in Microbiology;2013-07
4. The Glove-like Structure of the Conserved Membrane Protein TatC Provides Insight into Signal Sequence Recognition in Twin-Arginine Translocation;Structure;2013-05
5. Molecular dissection of TatC defines critical regions essential for protein transport and a TatB–TatC contact site;Molecular Microbiology;2012-07-13
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