Article
Identification of residues in DmsD for twin-arginine leader peptide binding, defined through random and bioinformatics-directed mutagenesis.
Biochemistry - 4 Mar 2008
Chan Catherine S, Winstone Tara M L, Chang Limei, Stevens Charles M, Workentine Matthew L, Li Haiming, Wei Ying, Ondrechen Mary J, Paetzel Mark, Turner Raymond J
Abstract excerpt
The twin-arginine translocase (Tat) system is used for the targeting and translocation of folded proteins across the cell membrane of most bacteria. Substrates of this system contain a conserved "twin-arginine" (RR) motif within their signal/leader peptide sequence. Many Tat substrates have their own system-specific chaperone called redox enzyme maturation proteins (REMPs). Here, we study the binding of DmsD, the...
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