Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone

Grant Buchanan; Julien Maillard; Sander B. Nabuurs; David J. Richardson; Tracy Palmer; Frank Sargent

doi:10.1016/j.febslet.2008.10.049

Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone

Grant Buchanan, Julien Maillard, Sander B. Nabuurs, David J. Richardson, Tracy Palmer, Frank Sargent

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

31 Citations (Scopus)

Abstract

The twin-arginine translocation (Tat) system is a bacterial protein targeting pathway. Tat-targeted proteins display signal peptides containing a distinctive SRRxFLK 'twin-arginine' motif. The Escherichia coli trimethylamine N-oxide reductase (TorA) bears a bifunctional Tat signal peptide, which directs protein export and serves as a binding site for the TorD biosynthetic chaperone. Here, the physical interaction between TorD and the TorA signal peptide was investigated. A single substitution within the TorA signal peptide (L31Q) was sufficient to impair TorD binding. Screening of a random torD mutant library identified a variant TorD protein (Q7L) that displayed increased binding affinity for the TorA signal peptide.

Original language	English
Pages (from-to)	3979-3984
Number of pages	6
Journal	FEBS Letters
Volume	582
Issue number	29
DOIs	https://doi.org/10.1016/j.febslet.2008.10.049
Publication status	Published - 10 Dec 2008

Keywords

Bacterial respiration
Bacterial protein targeting
Twin-arginine signal peptide
Tat proofreading chaperone
Protein-protein interaction
Site-directed mutagenesis
PROTEIN TRANSLOCATION PATHWAY
N-OXIDE REDUCTASE
ESCHERICHIA-COLI
DIRECTED MUTAGENESIS
EXPORT PATHWAY
TORD
MATURATION
MOLYBDOENZYME
INVOLVEMENT
BINDING

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10.1016/j.febslet.2008.10.049

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title = "Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone",

abstract = "The twin-arginine translocation (Tat) system is a bacterial protein targeting pathway. Tat-targeted proteins display signal peptides containing a distinctive SRRxFLK 'twin-arginine' motif. The Escherichia coli trimethylamine N-oxide reductase (TorA) bears a bifunctional Tat signal peptide, which directs protein export and serves as a binding site for the TorD biosynthetic chaperone. Here, the physical interaction between TorD and the TorA signal peptide was investigated. A single substitution within the TorA signal peptide (L31Q) was sufficient to impair TorD binding. Screening of a random torD mutant library identified a variant TorD protein (Q7L) that displayed increased binding affinity for the TorA signal peptide.",

keywords = "Bacterial respiration, Bacterial protein targeting, Twin-arginine signal peptide, Tat proofreading chaperone, Protein-protein interaction, Site-directed mutagenesis, PROTEIN TRANSLOCATION PATHWAY, N-OXIDE REDUCTASE, ESCHERICHIA-COLI, DIRECTED MUTAGENESIS, EXPORT PATHWAY, TORD, MATURATION, MOLYBDOENZYME, INVOLVEMENT, BINDING",

author = "Grant Buchanan and Julien Maillard and Nabuurs, {Sander B.} and Richardson, {David J.} and Tracy Palmer and Frank Sargent",

year = "2008",

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day = "10",

doi = "10.1016/j.febslet.2008.10.049",

language = "English",

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journal = "FEBS Letters",

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T1 - Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone

AU - Buchanan, Grant

AU - Maillard, Julien

AU - Nabuurs, Sander B.

AU - Richardson, David J.

AU - Palmer, Tracy

AU - Sargent, Frank

PY - 2008/12/10

Y1 - 2008/12/10

N2 - The twin-arginine translocation (Tat) system is a bacterial protein targeting pathway. Tat-targeted proteins display signal peptides containing a distinctive SRRxFLK 'twin-arginine' motif. The Escherichia coli trimethylamine N-oxide reductase (TorA) bears a bifunctional Tat signal peptide, which directs protein export and serves as a binding site for the TorD biosynthetic chaperone. Here, the physical interaction between TorD and the TorA signal peptide was investigated. A single substitution within the TorA signal peptide (L31Q) was sufficient to impair TorD binding. Screening of a random torD mutant library identified a variant TorD protein (Q7L) that displayed increased binding affinity for the TorA signal peptide.

AB - The twin-arginine translocation (Tat) system is a bacterial protein targeting pathway. Tat-targeted proteins display signal peptides containing a distinctive SRRxFLK 'twin-arginine' motif. The Escherichia coli trimethylamine N-oxide reductase (TorA) bears a bifunctional Tat signal peptide, which directs protein export and serves as a binding site for the TorD biosynthetic chaperone. Here, the physical interaction between TorD and the TorA signal peptide was investigated. A single substitution within the TorA signal peptide (L31Q) was sufficient to impair TorD binding. Screening of a random torD mutant library identified a variant TorD protein (Q7L) that displayed increased binding affinity for the TorA signal peptide.

KW - Bacterial respiration

KW - Bacterial protein targeting

KW - Twin-arginine signal peptide

KW - Tat proofreading chaperone

KW - Protein-protein interaction

KW - Site-directed mutagenesis

KW - PROTEIN TRANSLOCATION PATHWAY

KW - N-OXIDE REDUCTASE

KW - ESCHERICHIA-COLI

KW - DIRECTED MUTAGENESIS

KW - EXPORT PATHWAY

KW - TORD

KW - MATURATION

KW - MOLYBDOENZYME

KW - INVOLVEMENT

KW - BINDING

U2 - 10.1016/j.febslet.2008.10.049

DO - 10.1016/j.febslet.2008.10.049

M3 - Article

C2 - 19013157

SN - 0014-5793

VL - 582

SP - 3979

EP - 3984

JO - FEBS Letters

JF - FEBS Letters

IS - 29

ER -

Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone

Abstract

Keywords

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