Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.


Journal article



Publication Date





45 - 49


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