Identification of protein–protein interactions between the TatB and TatC subunits of the twin-arginine translocase system and respiratory enzyme specific chaperones

• Published in: Biochimica et biophysica acta Vol. 1858; no. 4; pp. 767 - 775
• Main Authors: Kuzniatsova, Lalita, Winstone, Tara M.L., Turner, Raymond J.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2016
• Subjects: Carrier Proteins - chemistry; Carrier Proteins - metabolism; Cell Membrane - chemistry; Cell Membrane - metabolism; Chaperones; DmsD; Escherichia coli - chemistry; Escherichia coli - enzymology; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - metabolism; Formate Dehydrogenases - chemistry; Formate Dehydrogenases - metabolism; Membrane Transport Proteins - chemistry; Membrane Transport Proteins - metabolism; Molecular Chaperones - chemistry; Molecular Chaperones - metabolism; molybdoenzymes; Protein Folding; Protein Interaction Maps; Protein Structure, Tertiary; Protein–protein interaction; REMP; Tat; Twin arginine translocase; Two-hybrid; RR; TMAO; DMSO; DTT; Tat; Chaperones; molybdoenzymes; Twin arginine translocase; Protein–protein interaction; Two-hybrid; REMP; BACTH; ITC; Kd; DmsD

The Twin-arginine translocation (Tat) pathway serves for translocation of fully folded proteins across the cytoplasmic membrane in bacterial and chloroplast thylakoid membranes. The Escherichia coli Tat system consists of three core components: TatA, TatB, and TatC. The TatB and TatC subunits form t...