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

Andrew P. Hinsley; Nicola R. Stanley; Tracy Palmer; Ben C. Berks

doi:10.1016/S0014-5793(01)02428-0

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

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

Research output: Contribution to journal › Article › peer-review

103 Citations (Scopus)

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.

Original language	English
Pages (from-to)	45-9
Number of pages	5
Journal	FEBS Letters
Volume	497
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(01)02428-0
Publication status	Published - 18 May 2001

Keywords

Sec-independent
Bacterial protein export
Tat pathway
Twin-arginine signal peptide
Tetrathionate reductase
Rieske protein

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10.1016/S0014-5793(01)02428-0

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title = "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.",

keywords = "Sec-independent, Bacterial protein export, Tat pathway, Twin-arginine signal peptide, Tetrathionate reductase, Rieske protein",

author = "Hinsley, \{Andrew P.\} and Stanley, \{Nicola R.\} and Tracy Palmer and Berks, \{Ben C.\}",

year = "2001",

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T1 - A naturally occurring bacterial Tat signal peptide lacking one of the 'invariant' arginine residues of the consensus targeting motif

AU - Hinsley, Andrew P.

AU - Stanley, Nicola R.

AU - Palmer, Tracy

AU - Berks, Ben C.

PY - 2001/5/18

Y1 - 2001/5/18

N2 - 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.

AB - 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.

KW - Sec-independent

KW - Bacterial protein export

KW - Tat pathway

KW - Twin-arginine signal peptide

KW - Tetrathionate reductase

KW - Rieske protein

U2 - 10.1016/S0014-5793(01)02428-0

DO - 10.1016/S0014-5793(01)02428-0

M3 - Article

C2 - 11376660

SN - 0014-5793

VL - 497

SP - 45

EP - 49

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

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

Abstract

Keywords

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