Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli.
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 'tw...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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2010
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| _version_ | 1797055211481595904 |
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| author | Palmer, T Berks, B Sargent, F |
| author_facet | Palmer, T Berks, B Sargent, F |
| author_sort | Palmer, T |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T19:07:51Z |
| format | Journal article |
| id | oxford-uuid:15c746a3-0d39-4cf4-9524-96259c39a68e |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:07:51Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:15c746a3-0d39-4cf4-9524-96259c39a68e2022-03-26T10:27:21ZAnalysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:15c746a3-0d39-4cf4-9524-96259c39a68eEnglishSymplectic Elements at Oxford2010Palmer, TBerks, BSargent, FThe 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. |
| spellingShingle | Palmer, T Berks, B Sargent, F Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli. |
| title | Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli. |
| title_full | Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli. |
| title_fullStr | Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli. |
| title_full_unstemmed | Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli. |
| title_short | Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli. |
| title_sort | analysis of tat targeting function and twin arginine signal peptide activity in escherichia coli |
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