Abstract:
: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_name
FEBS Lettjournal_title
FEBS lettersauthors
Hinsley AP,Stanley NR,Palmer T,Berks BCdoi
10.1016/s0014-5793(01)02428-0keywords:
subject
Has Abstractpub_date
2001-05-18 00:00:00pages
45-9issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02428-0journal_volume
497pub_type
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