- Investigating lipoprotein biogenesis and function in the model Gram-positive bacterium Streptomyces coelicolormmi_7261 943..957
- Abstract The Escherichia coli Tat protein export path-way transports folded proteins synthesized with N-termi-
- Abstract The mob genes of several bacteria have been implicated in the conversion of molybdopterin to molyb-
- Characterization and Membrane Assembly of the TatA Component of the Escherichia coli Twin-Arginine Protein Transport System
- MicroCommentary A new way out: protein localization on the bacterial cell
- Arch Microbiol (2008) 190:685696 DOI 10.1007/s00203-008-0420-4
- Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins
- COMMUNICATION A Facile Reporter System for the Experimental
- Arch Microbiol (2008) 189:597604 DOI 10.1007/s00203-008-0356-8
- JOURNAL OF BACTERIOLOGY, Sept. 2004, p. 63116315 Vol. 186, No. 18 0021-9193/04/$08.00 0 DOI: 10.1128/JB.186.18.63116315.2004
- |Research Focus Light traffic
- JOURNAL OF BACTERIOLOGY, Jan. 2004, p. 366373 Vol. 186, No. 2 0021-9193/04/$08.00 0 DOI: 10.1128/JB.186.2.366373.2004
- Cysteine Scanning Mutagenesis and Disulfide Mapping Studies of the TatA Component of the Bacterial Twin
- The Entire N-Terminal Half of TatC is Involved in Twin-Arginine Precursor Eva Holzapfel,,,|| Gottfried Eisner,,|, Meriem Alami,,X Claire M. L. Barrett,O Grant Buchanan,#,3 Iris Luke,,[
- Export Pathway Selectivity of Escherichia coli Twin Arginine Translocation Signal Peptides*S
- physiology and biochemistry of Tat transport To cite this pdf: Berks, B.C., Palmer, T. and Sargent, F. (2003) Advances in Microbial Physiology 47, 187-254
- Molecular Microbiology (2003) 49(5), 13771390 doi:10.1046/j.1365-2958.2003.03642.x 2003 Blackwell Publishing Ltd
- The Escherichia coli twin-arginine translocase: conserved residues of TatA and TatB family components involved in protein transport
- How Escherichia coli Is Equipped to Oxidize Hydrogen under Different Redox Conditions*S
- The twin arginine protein transport pathway exports multiple virulence proteins in the plant pathogen
- Subunit composition and in vivo substrate-binding characteristics of Escherichia coli Tat protein complexes
- Cysteine-scanning Mutagenesis and Disulfide Mapping Studies of the Conserved Domain of the Twin-arginine
- 200 / Molecular Plant-Microbe Interactions MPMI Vol. 19, No. 2, 2006, pp. 200212. DOI: 10.1094/MPMI-19-0200. 2006 The American Phytopathological Society
- M I N I R E V I E W Pathndersandtrailblazers:a prokaryotic targetingsystemfor
- JOURNAL OF BACTERIOLOGY, Nov. 2002, p. 58715879 Vol. 184, No. 21 0021-9193/02/$04.00 0 DOI: 10.1128/JB.184.21.58715879.2002
- Genetic Analysis of the Twin Arginine Translocator Secretion Pathway in Bacteria*
- Crystal Structure of the Acid-Induced Arginine Decarboxylase from Escherichia coli: Reversible Decamer Assembly Controls
- JOURNAL OF BACTERIOLOGY, Aug. 2009, p. 47324749 Vol. 191, No. 15 0021-9193/09/$08.00 0 doi:10.1128/JB.00136-09
- Ways & Means The Orientation of a Tandem POTRA Domain Pair, of
- Structural analysis of substrate binding by the TatBC component of the twin-arginine protein
- This article was published in the above mentioned Springer issue. The material, including all portions thereof, is protected by copyright;
- Export of complex cofactor-containing proteins by the bacterial Tat pathway
- Characterisation of Tat protein transport complexes carrying inactivating mutations
- JOURNAL OF BACTERIOLOGY, 0021-9193/01/$04.00 0 DOI: 10.1128/JB.183.5.18011804.2001
- 2002 Blackwell Science Ltd Functional complexity of the twin-arginine translocase
- JOURNAL OF BACTERIOLOGY, July 2008, p. 51275131 Vol. 190, No. 14 0021-9193/08/$08.00 0 doi:10.1128/JB.00395-08
- JOURNAL OF BACTERIOLOGY, Aug. 2007, p. 54825494 Vol. 189, No. 15 0021-9193/07/$08.00 0 doi:10.1128/JB.00647-07
- TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli
- SGM Special Moving folded proteins across the bacterial cell
- Biochemical and Structural Analysis of the Molybdenum Cofactor Biosynthesis Protein MobA*
- In vivo Dissection of the Tat Translocation Pathway in Escherichia coli
- Lipoprotein biogenesis in Gram-positive bacteria: knowing when to
- Coordinating assembly and export of complex bacterial proteins
- Abstract The Tat protein-export system serves to trans-locate folded proteins, often containing redox cofactors,
- Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone
- International Hydrogenases Conference 2004 105 Common principles in the biosynthesis
- Remnant signal peptides on non-exported enzymes: implications for the evolution of
- Molecular Microbiology (2003) 48(5), 11831193 doi:10.1046/j.1365-2958.2003.03504.x 2003 Blackwell Publishing Ltd
- 2002 Blackwell Science Ltd Behaviour of topological marker proteins targeted to
- An Essential Role for the DnaK Molecular Chaperone in Stabilizing Over-expressed Substrate Proteins of the
- Oligomeric Properties and Signal Peptide Binding by Escherichia coli Tat Protein Transport Complexes
- BioMed Central Page 1 of 9
- A naturally occurring bacterial Tat signal peptide lacking one of the `invariant' arginine residues of the consensus targeting motif
- Novel Phenotypes of Escherichia coli tat Mutants Revealed by Global Gene Expression and Phenotypic Analysis*S
- Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway
- Protein targeting by the bacterial twin-arginine translocation (Tat) pathway
- StreptomycesThe twin-arginine translocation pathway is a major route of protein export in Pohlschrder, and Tracy Palmer
- JOURNAL OF BACTERIOLOGY, Apr. 2005, p. 29202925 Vol. 187, No. 8 0021-9193/05/$08.00 0 doi:10.1128/JB.187.8.29202925.2005
- Eur. J. Biochem. 268, 33613367 (2001) q FEBS 2001 P R I O R I T Y PA P E R
- JOURNAL OF BACTERIOLOGY, 0021-9193/01/$04.00 0 DOI: 10.1128/JB.183.1.139144.2001
- BioMed Central Page 1 of 12
- with a sinking motion over the winter pole. This descent causes the concentration of sev-
- R E V I E W A R T I C L E The complexextracellular biologyof Streptomyces
- Structural diversity in twin-arginine signal peptide-binding proteins
- The TatA component of the twin-arginine protein transport system forms channel complexes
