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The entire N-terminal half of TatC is involved in twin-arginine precursor binding
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Holzapfel, Eva, Eisner, Gottfried, Alami, Meriem, Barrett, Claire M. L., Buchanan, Grant, Lueke, Iris, Betton, Jean-Michel, Robinson, Colin, Palmer, Tracy, Moser, Michael and Mueller, Matthias (2007) The entire N-terminal half of TatC is involved in twin-arginine precursor binding. Biochemistry, Vol.46 (No.10). pp. 2892-2898. doi:10.1021/bi062205b ISSN 0006-2960.
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Official URL: http://dx.doi.org/10.1021/bi062205b
Abstract
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.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) > Biological Sciences ( -2010) | ||||
Journal or Publication Title: | Biochemistry | ||||
Publisher: | American Chemical Society | ||||
ISSN: | 0006-2960 | ||||
Official Date: | 13 March 2007 | ||||
Dates: |
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Volume: | Vol.46 | ||||
Number: | No.10 | ||||
Number of Pages: | 7 | ||||
Page Range: | pp. 2892-2898 | ||||
DOI: | 10.1021/bi062205b | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
Data sourced from Thomson Reuters' Web of Knowledge
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