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
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2010.10.043

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 with and without a leader cleavage site, mature protein) were assayed for interaction with their REMPs. All REMPs bound their preprotein substrates independent of the cleavage site. Some showed binding to either the leader or mature region, whereas in one case only the preprotein bound its REMP. The absence of Tat also influenced the amount of chaperone–substrate interaction. MINT- 8047497: FdhE (uniprotkb: P13024) and FdoG (uniprotkb: P32176) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT- 8046441: HybO (uniprotkb: P69741) and HybE (uniprotkb: P0AAN1) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT- 8046375: DmsA (uniprotkb: P18775) and DmsD (uniprotkb: P69853) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT- 8046425: TorA (uniprotkb: P33225) and TorD (uniprotkb: P36662) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT- 8046393: NarJ (uniprotkb: P0AF26) and NarG (uniprotkb: P09152) physically interact (MI: 0915) by two hybrid (MI: 0018) MINT- 8046409: NapD (uniprotkb: P0A9I5) and NapA (uniprotkb: P33937) physically interact (MI: 0915) by two hybrid (MI: 0018)