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• W2022372636 abstract "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." @default.
• W2022372636 created "2016-06-24" @default.
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• W2022372636 date "2010-10-23" @default.
• W2022372636 modified "2023-10-03" @default.
• W2022372636 title "Comparing system-specific chaperone interactions with their Tat dependent redox enzyme substrates" @default.
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• W2022372636 doi "https://doi.org/10.1016/j.febslet.2010.10.043" @default.
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