About: The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting inEscherichia coli

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scientific article published in Journal of Biological Chemistry

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) wüsseschaftlicher Artikel, wo im April 2000 veröffentlicht worden isch (gsw) наукова стаття, опублікована у квітні 2000 (uk) im April 2000 veröffentlichter wissenschaftlicher Artikel (de) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q57839654-1EF17D93-D9B4-4AB0-B678-3E3EF8571162
publication date	2000-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57839654-E8A1EC10-222C-472B-BCC1-D85EE4D8CDA1
language of work or name	English
cites work	wds:Q57839654-0BE4C1DB-D914-4CC9-88A6-5FCE74BCFCB3 wds:Q57839654-20C3B1E7-6363-4129-9E02-57CE44F98C72 wds:Q57839654-23052D2A-0606-4690-978C-52E860C12E6F wds:Q57839654-389B0C3A-C49D-4A19-92BB-A508F9DB3EAF wds:Q57839654-3A6F83FE-4921-4106-B074-352102C476B0 wds:Q57839654-41CC0EDD-AC3E-4705-8D78-3A8245857906 wds:Q57839654-47BBB1DB-74BC-4D21-AF8F-C386863F393F wds:Q57839654-53EB46F9-01CF-4FCB-AAE5-0771FF7F04CC wds:Q57839654-651B507F-3C23-4D16-98E5-BFC34BA32ADB wds:Q57839654-66C4AC1B-1315-4414-9510-F8843A3EF6A2 wds:Q57839654-69A845FC-EBDF-4654-97DB-DC3258654551 wds:Q57839654-6D4EB55F-4A00-48D5-8788-97478232CD2D wds:Q57839654-710A2F46-1591-4A4D-8D3C-056C7449D088 wds:Q57839654-7DD32C30-9FE6-4D55-AC76-694BC4072D4B wds:Q57839654-878007F9-179D-4D15-B613-FDB39281DDD1 wds:Q57839654-87D4D0ED-0181-4ADD-A3ED-B4EDF1944012 wds:Q57839654-8ADF18C2-DA14-41D5-81C4-79B54039BE40 wds:Q57839654-90ACF78D-D407-4F88-B40B-6BEE3D57E616 wds:Q57839654-942DD362-8AF4-400B-A7C0-09CA2D6125AF wds:Q57839654-944AF433-7D52-4A79-9C67-19B3F3C03F84 wds:Q57839654-9EF684F9-4069-4DBB-A302-8CBE095A9932 wds:Q57839654-A1A82021-5C85-46EA-930B-307DE92990D6 wds:Q57839654-A3E2A7D8-FB80-4E6D-BDBC-B56280498122 wds:Q57839654-AF758AD6-565F-4231-B676-C278134BFC70 wds:Q57839654-B130E7FC-CEA1-481A-A7CB-24CF38D404CF wds:Q57839654-B1321B66-EA3F-46F2-8C5B-C2C4F28FE478 wds:Q57839654-B4399E57-B78C-4867-889E-8DFD6DF7B32E wds:Q57839654-B878B075-673E-4409-9BA4-C4B3B972ACF2 wds:Q57839654-C19BCD2A-4E59-4C4C-BB5B-4170FB419CB4 wds:Q57839654-C5CF0132-790C-4A8F-90B9-F88C05E66C9B wds:Q57839654-C665C994-72EB-4A91-811F-053CC9398F7D wds:Q57839654-E90C261A-F915-437B-95B2-C5F196A60BB0
cites work	New method for generating deletions and gene replacements in Escherichia coli Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a beta-lactamase fusion protein A signal peptide that directs non-Sec transport in bacteria also directs efficient and exclusive transport on the thylakoid Delta pH pathway Bacterial proteins carrying twin-R signal peptides are specifically targeted by the delta pH-dependent transport machinery of the thylakoid membrane system The efficient export of NADP-containing glucose-fructose oxidoreductase to the periplasm of Zymomonas mobilis depends both on an intact twin-arginine motif in the signal peptide and on the generation of a structural export signal induced by cofactor Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences Signal sequences. The limits of variation Protein import and routing systems of chloroplasts Competition between Sec- and TAT-dependent protein translocation in Escherichia coli Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes The genetic map of the filamentous bacteriophage f1 A common export pathway for proteins binding complex redox cofactors? Targeting determinants and proposed evolutionary basis for the Sec and the Delta pH protein transport systems in chloroplast thylakoid membranes Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein. In vitro insertional mutagenesis with a selectable DNA fragment Gene organization in the region containing a new gene involved in chromosome partition in Escherichia coli Signal peptides: exquisitely designed transport promoters Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli A novel sec-independent periplasmic protein translocation pathway in Escherichia coli The Tat protein export pathway Pathway specificity for a delta pH-dependent precursor thylakoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria. A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins. Targeting signals for a bacterial Sec-independent export system direct plant thylakoid import by the ΔpH pathway Structures of N-termini of helices in proteins Targeting of thylakoid proteins by the delta pH-driven twin-arginine translocation pathway requires a specific signal in the hydrophobic domain in conjunction with the twin-arginine motif Alteration of the amino terminus of the mature sequence of a periplasmic protein can severely affect protein export in Escherichia coli Co-translocation of a Periplasmic Enzyme Complex by a Hitchhiker Mechanism through the Bacterial Tat Pathway Lack of copper insertion into unprocessed cytoplasmic nitrous oxide reductase generated by an R20D substitution in the arginine consensus motif of the signal peptide. The role of the twin-arginine motif in the signal peptide encoded by the hydA gene of the hydrogenase from wolinella succinogenes Evidence against the double-arginine motif as the only determinant for protein translocation by a novel Sec-independent pathway in Escherichia coli
author name string	wds:Q57839654-AE350757-FF8D-4A87-8BA3-4DF9CCAF0406
author name string	N R Stanley
rdfs:label	The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting inEscherichia coli (en) The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting inEscherichia coli (nl)
skos:prefLabel	The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting inEscherichia coli (en) The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting inEscherichia coli (nl)
name	The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting inEscherichia coli (en) The Twin Arginine Consensus Motif of Tat Signal Peptides Is Involved in Sec-independent Protein Targeting inEscherichia coli (nl)
author	wds:Q57839654-50142919-8D1F-402D-AB5F-F84C55AD0EBE wds:Q57839654-C1A19D0D-6F76-4EC1-BBBA-91BE36D407DD
author	Tracy Palmer Ben C Berks
title	wds:Q57839654-18E6DB18-3EA8-400E-8646-02F9F71B7101
title	The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli (en)
page(s)	wds:Q57839654-0717D365-B5B3-4ED2-AB41-F7D255C6C677
page(s)	11591-11596
instance of	wds:Q57839654-1163CDFD-6208-4534-B253-C94C63010309
instance of	scholarly article
main subject	wds:Q57839654-4766CED2-9D06-476A-9DF3-179F41D6C3B0
main subject	Escherichia coli
PubMed ID	wds:Q57839654-C6C33C50-6B6E-4ADB-A747-620D1E6B202F
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10766774
PubMed ID	10766774
published in	wds:Q57839654-437DBDDC-6E54-4A9F-80A6-FE02F5BE0E75

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