TatA and TatB generate a hydrophobic mismatch important for the function and assembly of the Tat translocon in Escherichia coli

• Published in: The Journal of biological chemistry Vol. 298; no. 9; p. 102236
• Main Authors: Mehner-Breitfeld, Denise, Ringel, Michael T., Tichy, Daniel Alexander, Endter, Laura J., Stroh, Kai Steffen, Lünsdorf, Heinrich, Risselada, Herre Jelger, Brüser, Thomas
• Format: Journal Article
• Language: English
• Published: Elsevier Inc 01.09.2022; American Society for Biochemistry and Molecular Biology
• Subjects: computational biology; hydrophobic mismatch; membrane proteins; membrane thinning; metal-tagging transmission electron microscopy (METTEM); protein translocation; stress response; Tat system; computational biology; COM; BN-PAGE; Tat; TMH; protein translocation; PEELS; membrane proteins; stress response; hydrophobic mismatch; METTEM; APH; Tat system; metal-tagging transmission electron microscopy (METTEM); membrane thinning

The twin-arginine translocation (Tat) system serves to translocate folded proteins across energy-transducing membranes in bacteria, archaea, plastids, and some mitochondria. In Escherichia coli, TatA, TatB, and TatC constitute functional translocons. TatA and TatB both possess an N-terminal transmem...