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Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli.

Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli.

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Original languageEnglish
TitleProtein secretion
Subtitlemethods and protocols
EditorsAnastassios Economou
PublisherHumana Press
Publication date2010
Pages191-216
Number of pages26
ISBN (Electronic)9781603274128
ISBN (Print)9781603271677
DOIs
StatePublished

Publication series

NameMethods in Molecular Biology
PublisherHumana Press
Volume619
ISSN (Print)1064-3745

Abstract

The Tat system is a protein export system dedicated to the transport of folded proteins across the prokaryotic cytoplasmic membrane and the thylakoid membrane of plant chloroplasts. Proteins are targeted for export by the Tat system via N-terminal signal peptides harbouring an S-R-R-x-F-L-K 'twin-arginine' motif. In this chapter qualitative and quantitative assays for native Tat substrates in the model organism Escherichia coli are described. Genetic screening methods designed to allow the rapid positive selection of Tat signal peptide activity and the first positive selection for mutations that inactivate the Tat pathway are also presented. Finally isothermal titration calorimetry (ITC) methods for measuring the affinity of twin-arginine signal peptide-chaperone interactions are discussed.

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