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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2003-8-27
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pubmed:abstractText |
A group of bacterial exported proteins are synthesized with N-terminal signal peptides containing a SRRxFLK 'twin-arginine' amino acid motif. Proteins bearing twin-arginine signal peptides are targeted post-translationally to the twin-arginine translocation (Tat) system which transports folded substrates across the inner membrane. In Escherichia coli, most integral inner membrane proteins are assembled by a co-translational process directed by SRP/FtsY, the SecYEG translocase, and YidC. In this work we define a novel class of integral membrane proteins assembled by a Tat-dependent mechanism. We show that at least five E. coli Tat substrate proteins contain hydrophobic C-terminal transmembrane helices (or 'C-tails'). Fusions between the identified transmembrane C-tails and the exclusively Tat-dependent reporter proteins TorA and SufI render the resultant chimeras membrane-bound. Export-linked signal peptide processing and membrane integration of the chimeras is shown to be both Tat-dependent and YidC-independent. It is proposed that the mechanism of membrane integration of proteins by the Tat system is fundamentally distinct from that employed for other bacterial inner membrane proteins.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP-Binding Cassette Transporters,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases, N-Demethylating,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SufI protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/YIDC protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/nikA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/trimethylamine dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/twin-arginine translocase complex...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0950-382X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1377-90
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12940994-ATP-Binding Cassette Transporters,
pubmed-meshheading:12940994-Artificial Gene Fusion,
pubmed-meshheading:12940994-Carrier Proteins,
pubmed-meshheading:12940994-Cell Membrane,
pubmed-meshheading:12940994-Escherichia coli,
pubmed-meshheading:12940994-Escherichia coli Proteins,
pubmed-meshheading:12940994-Genes, Reporter,
pubmed-meshheading:12940994-Membrane Proteins,
pubmed-meshheading:12940994-Membrane Transport Proteins,
pubmed-meshheading:12940994-Oxidoreductases, N-Demethylating,
pubmed-meshheading:12940994-Protein Sorting Signals,
pubmed-meshheading:12940994-Protein Transport,
pubmed-meshheading:12940994-Recombinant Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
A subset of bacterial inner membrane proteins integrated by the twin-arginine translocase.
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pubmed:affiliation |
Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich, NR4 7TJ, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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