TY  - JOUR
T1  - Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase
A1  - Maldonado ,Barbara
A1  - Kneuper,Holger
A1  - Buchanan,Grant
A1  - Hatzixanthis,Kostas
A1  - Sargent,Frank
A1  - Berks,Ben C.
A1  - Palmer,Tracy
AU  - Maldonado ,Barbara
AU  - Kneuper,Holger
AU  - Buchanan,Grant
AU  - Hatzixanthis,Kostas
AU  - Sargent,Frank
AU  - Berks,Ben C.
AU  - Palmer,Tracy
PY  - 2011/2/4
Y1  - 2011/2/4
N2  - <p>The twin arginine protein transport (Tat) system transports folded proteins across cytoplasmic membranes of bacteria and thylakoid membranes of plants, and in Escherichia coli it comprises TatA, TatB and TatC components. In this study we show that the membrane extrinsic domain of TatB forms parallel contacts with at least one other TatB protein. Truncation of the C-terminal two thirds of TatB still allows complex formation with TatC, although protein transport is severely compromised. We were unable to isolate transport-inactive single codon substitution mutations in tatB suggesting that the precise amino acid sequence of TatB is not critical to its function.</p><p>Structured summary:</p><p>TatA physically interacts with TatA by two hybrid (View interaction)</p><p>TatB and TatC bind by molecular sieving (View interaction)</p><p>TatB physically interacts with TatB by two hybrid (View Interaction 1, 2) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</p>
AB  - <p>The twin arginine protein transport (Tat) system transports folded proteins across cytoplasmic membranes of bacteria and thylakoid membranes of plants, and in Escherichia coli it comprises TatA, TatB and TatC components. In this study we show that the membrane extrinsic domain of TatB forms parallel contacts with at least one other TatB protein. Truncation of the C-terminal two thirds of TatB still allows complex formation with TatC, although protein transport is severely compromised. We were unable to isolate transport-inactive single codon substitution mutations in tatB suggesting that the precise amino acid sequence of TatB is not critical to its function.</p><p>Structured summary:</p><p>TatA physically interacts with TatA by two hybrid (View interaction)</p><p>TatB and TatC bind by molecular sieving (View interaction)</p><p>TatB physically interacts with TatB by two hybrid (View Interaction 1, 2) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</p>
KW  - Protein transport
KW  - Twin arginine signal peptide
KW  - Tat pathway
KW  - TatB
KW  - Protein:protein interaction
KW  - Mutagenesis
KW  - SEC-INDEPENDENT PROTEIN
KW  - CYSTEINE-SCANNING MUTAGENESIS
KW  - BACTERIAL 2-HYBRID SYSTEM
KW  - ESCHERICHIA-COLI
KW  - TRANSPORT SYSTEM
KW  - SIGNAL PEPTIDE
KW  - EXPORT PATHWAY
KW  - BINDING
KW  - COMPLEXES
KW  - RESIDUES
U2  - 10.1016/j.febslet.2011.01.016
DO  - 10.1016/j.febslet.2011.01.016
M1  - Article
JO  - FEBS Letters
JF  - FEBS Letters
SN  - 0014-5793
IS  - 3
VL  - 585
SP  - 478
EP  - 484
ER  -