Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-4-26
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1940-6029
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
619
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
191-216
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli.
pubmed:affiliation
Division of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee, Scotland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't