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Currently described substrates of the bacterial Tat protein transport system are directed for export by signal peptides containing a pair of invariant arginine residues. The signal peptide of the TtrB subunit of Salmonella enterica tetrathionate reductase contains a single arginine residue but is nevertheless able to mediate Tat pathway transport. This naturally occurring example of a Tat signal peptide lacking a consensus arginine pair expands the range of sequences that can target a protein to the Tat pathway. The possible implications of this finding for the assembly of electron transfer complexes containing Rieske proteins in plant organelles are discussed.

Type

Journal article

Journal

FEBS Lett

Publication Date

18/05/2001

Volume

497

Pages

45 - 49

Keywords

Amino Acid Motifs, Amino Acid Substitution, Arginine, Bacterial Proteins, Consensus Sequence, Molecular Sequence Data, Mutagenesis, Site-Directed, Oxidoreductases, Protein Sorting Signals, Protein Transport, Recombinant Fusion Proteins, Salmonella enterica, Sequence Homology, Amino Acid, Structure-Activity Relationship, Subcellular Fractions