The Hydrophobic Core of Twin-Arginine Signal Sequences Orchestrates Specific Binding to Tat-Pathway Related Chaperones

Basis of recognition between the NarJ chaperone and the N-terminus of the NarG subunit from Escherichia coli nitrate reductase

(2010) Silva Zakian et al.   FEBS Journal

Intrinsic GTPase activity of a bacterial twin-arginine translocation proofreading chaperone induced by domain swapping

(2010) David Guymer et al.   FEBS Journal

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

(2010) Catherine S. Chan et al.   FEBS LETTERS

Differential Interactions between Tat-Specific Redox Enzyme Peptides and Their Chaperones

(2009) C. S. Chan et al.   JOURNAL OF BACTERIOLOGY

Structural Analysis of a Monomeric Form of the Twin-Arginine Leader Peptide Binding Chaperone Escherichia coli DmsD

(2009) Charles M. Stevens et al.   JOURNAL OF MOLECULAR BIOLOGY

Interconvertibility of lipid- and translocon-bound forms of the bacterial Tat precursor pre-SufI

(2009) Umesh K. Bageshwar et al.   MOLECULAR MICROBIOLOGY

Identification of Residues in DmsD for Twin-Arginine Leader Peptide Binding, Defined through Random and Bioinformatics-Directed Mutagenesis†

(2008) Catherine S. Chan et al.   BIOCHEMISTRY

Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone

(2008) Grant Buchanan et al.   FEBS LETTERS

Characterization and multiple molecular forms of TorD from Shewanella massilia, the putative chaperone of the molybdoenzyme TorA

(2002) Samuel Tranier et al.   PROTEIN SCIENCE