A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif.
FEBS Lett
; 497(1): 45-9, 2001 May 18.
Article
em En
| MEDLINE
| ID: mdl-11376660
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.
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Base de dados:
MEDLINE
Assunto principal:
Oxirredutases
/
Sinais Direcionadores de Proteínas
/
Motivos de Aminoácidos
Idioma:
En
Ano de publicação:
2001
Tipo de documento:
Article