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

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 Lett

journal_title

FEBS letters

authors

Hinsley AP,Stanley NR,Palmer T,Berks BC

doi

10.1016/s0014-5793(01)02428-0

keywords:

subject

Has Abstract

pub_date

2001-05-18 00:00:00

pages

45-9

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02428-0

journal_volume

497

pub_type

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