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The Escherichia coli TatABC system and a Bacillus subtilis TatAC-type system recognise three distinct targeting determinants in twin-arginine signal peptides
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Mendel, Sharon, McCarthy, Andrew, Barnett, James P., Dr., Eijlander, Robyn T., Nenninger, Anja, Kuipers, O. P. and Robinson, Colin (2008) The Escherichia coli TatABC system and a Bacillus subtilis TatAC-type system recognise three distinct targeting determinants in twin-arginine signal peptides. Journal of Molecular Biology, Volume 375 (Number 3). pp. 661-672. doi:10.1016/j.jmb.2007.09.087
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Official URL: http://dx.doi.org/10.1016/j.jmb.2007.09.087
Abstract
The Tat system transports folded proteins across bacterial and thylakoid membranes. In Gram-negative organisms, it is encoded by tatABC genes and the system recognizes substrates bearing signal peptides with a conserved twin-arginine motif. Most Gram-positive organisms lack a tatB gene, indicating major differences in organisation. and/or mechanism. Here,, we have characterized the essential targeting determinants that are recognized by a Bacillus subtilis TatAC-type system, TatAdCd. Substitution by lysine of either of the twin-arginine residues in the TorA signal peptide can be tolerated, but the presence of twin-lysine residues blocks export completely. We show that additional determinants can be as important as the twin-arginine motif. Replacement of the -1 serine by alanine, in either the TorA or DmsA signal peptide, almost blocks export by either the B. subtilis TatAdCd or Escherichia coli TatABC systems, firmly establishing the importance of this -1 residue in these signal peptides. Surprisingly, the +2 leucine in the DmsA signal peptide (sequence SRRGLV) appears to play an equally important role and substitution by alardine or phenylalanine blocks export by both the B. subtilis and E. coli systems. These data identify three distinct determinants, whose importance varies depending on the signal peptide in question. The data also show that the B. subtilis TatAdCd and E. coli TatABC systems recognize very similar determinants within their target peptides, and exhibit surprisingly similar responses to mutations within these determinants. (c) 2007 Published by Elsevier Ltd.
| Item Type: | Journal Article | ||||
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| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology Q Science > QR Microbiology |
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| Divisions: | Faculty of Science > Chemistry Faculty of Science > Life Sciences (2010- ) Faculty of Science > Molecular Organisation and Assembly in Cells (MOAC) Faculty of Science > Centre for Systems Biology |
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| Library of Congress Subject Headings (LCSH): | Translocation (Genetics), Peptides, Biological transport, Proteins, Escherichia coli -- Physiology, Bacillus subtilis -- Physiology | ||||
| Journal or Publication Title: | Journal of Molecular Biology | ||||
| Publisher: | Academic Press | ||||
| ISSN: | 0022-2836 | ||||
| Official Date: | 18 January 2008 | ||||
| Dates: |
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| Volume: | Volume 375 | ||||
| Number: | Number 3 | ||||
| Number of Pages: | 12 | ||||
| Page Range: | pp. 661-672 | ||||
| DOI: | 10.1016/j.jmb.2007.09.087 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | European Union (EU), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) | ||||
| Grant number: | LSHC-CT2004-05257 (EU) |
Data sourced from Thomson Reuters' Web of Knowledge
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