A naturally occurring bacterial Tat signal peptide lacking one of the ‘invariant’ arginine residues of the consensus targeting motif

FEBS Letters

Hinsley, Andrew P.¹  Stanley, Nicola R.¹  Berks, Ben C.¹  Palmer, Tracy¹ 

[1] Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK

关键词: Sec-independent;    Bacterial protein export;    Tat pathway;    Twin–arginine signal peptide;    Tetrathionate reductase;    Rieske protein;   

DOI  :  10.1016/S0014-5793(01)02428-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown