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

被引：91

作者：

Hinsley, AP

Stanley, NR

Palmer, T

Berks, BC ^{[1
]}

机构：

[1] Univ E Anglia, Sch Biol Sci, Ctr Metalloprot Spect & Biol, Norwich NR4 7TJ, Norfolk, England

[2] John Innes Ctr Plant Sci Res, Dept Mol Microbiol, Norwich NR4 7UH, Norfolk, England

来源：

FEBS LETTERS | 2001年 / 497卷 / 01期

关键词：

sec-independent; bacterial protein export; Tat pathway; twin-arginine signal peptide; tetrathionate reductase; Rieske protein;

D O I：

10.1016/S0014-5793(01)02428-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：45 / 49

页数：5

共 22 条

[11] The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor binding [J].