The entire N-terminal half of TatC is involved in twin-arginine precursor binding.
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The entire N-terminal half of TatC is involved in twin-arginine precursor binding. / Holzapfel, Eva; Eisner, Gottfried; Alami, Meriem; Barrett, Claire M L; Buchanan, Grant; Lüke, Iris; Betton, Jean-Michel; Robinson, Colin; Palmer, Tracy; Moser, Michael; Müller, Matthias.
in: BIOCHEMISTRY-US, Jahrgang 46, Nr. 10, 10, 2007, S. 2892-2898.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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T1 - The entire N-terminal half of TatC is involved in twin-arginine precursor binding.
AU - Holzapfel, Eva
AU - Eisner, Gottfried
AU - Alami, Meriem
AU - Barrett, Claire M L
AU - Buchanan, Grant
AU - Lüke, Iris
AU - Betton, Jean-Michel
AU - Robinson, Colin
AU - Palmer, Tracy
AU - Moser, Michael
AU - Müller, Matthias
PY - 2007
Y1 - 2007
N2 - Translocation of twin-arginine precursor proteins across the cytoplasmic membrane of Escherichia coli requires the three membrane proteins TatA, TatB, and TatC. TatC and TatB were shown to be involved in precursor binding. We have analyzed in vitro a number of single alanine substitutions in tatC that were previously shown to compromise in vivo the function of the Tat translocase. All tatC mutants that were defective in precursor translocation into cytoplasmic membrane vesicles concomitantly interfered with precursor binding not only to TatC but also to TatB. Hence structural changes of TatC that affect precursor targeting simultaneously abolish engagement of the twin-arginine signal sequence with TatB and block the formation of a functional Tat translocase. Since these phenotypes were observed for tatC mutations spread over the first half of TatC, this entire part of the molecule must globally be involved in precursor binding.
AB - Translocation of twin-arginine precursor proteins across the cytoplasmic membrane of Escherichia coli requires the three membrane proteins TatA, TatB, and TatC. TatC and TatB were shown to be involved in precursor binding. We have analyzed in vitro a number of single alanine substitutions in tatC that were previously shown to compromise in vivo the function of the Tat translocase. All tatC mutants that were defective in precursor translocation into cytoplasmic membrane vesicles concomitantly interfered with precursor binding not only to TatC but also to TatB. Hence structural changes of TatC that affect precursor targeting simultaneously abolish engagement of the twin-arginine signal sequence with TatB and block the formation of a functional Tat translocase. Since these phenotypes were observed for tatC mutations spread over the first half of TatC, this entire part of the molecule must globally be involved in precursor binding.
M3 - SCORING: Zeitschriftenaufsatz
VL - 46
SP - 2892
EP - 2898
JO - BIOCHEMISTRY-US
JF - BIOCHEMISTRY-US
SN - 0006-2960
IS - 10
M1 - 10
ER -