Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates

• Published in: FEBS letters Vol. 584; no. 22; pp. 4553 - 4558
• Main Authors: Chan, Catherine S., Chang, Limei, Winstone, Tara M.L., Turner, Raymond J.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 19.11.2010
• Subjects: Amino Acid Motifs; Arginine; Bacterial two-hybrid; BACTH; Catalytic Domain; Escherichia coli - enzymology; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - metabolism; Leader sequence; Membrane Transport Proteins - chemistry; Membrane Transport Proteins - metabolism; Molecular Chaperones - metabolism; Oxidoreductases - chemistry; Oxidoreductases - metabolism; Protein Binding; Protein maturation; Protein Subunits - chemistry; Protein Subunits - metabolism; redox enzyme maturation protein; REMP; Substrate Specificity; System specific chaperone; Tat; Twin arginine translocase; Twin-arginine translocase system; REMP; Leader sequence; System specific chaperone; Bacterial two-hybrid; Tat; BACTH; Twin-arginine translocase system; Twin arginine translocase; Protein maturation

Redox enzyme substrates of the twin-arginine translocation (Tat) system contain a RR-motif in their leader peptide and require the assistance of chaperones, redox enzyme maturation proteins (REMPs). Here various regions of the RR-containing oxidoreductase subunit (leader peptide, full preprotein wit...