Ontology highlight
ABSTRACT:
SUBMITTER: Chan CS
PROVIDER: S-EPMC3285697 | biostudies-literature | 2010 Nov
REPOSITORIES: biostudies-literature
Chan Catherine S CS Chang Limei L Winstone Tara M L TM Turner Raymond J RJ
FEBS letters 20101026 22
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 t ...[more]