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A minimal tat system from a gram-positive organism - A bifunctional TatA subunit participates in discrete TatAC and TatA complexes
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Barnett, James P., Dr., Eijlander, Robyn T., Kuipers, O. P. and Robinson, Colin (2008) A minimal tat system from a gram-positive organism - A bifunctional TatA subunit participates in discrete TatAC and TatA complexes. Journal of Biological Chemistry, Volume 283 (Number 5). pp. 2534-2542. doi:10.1074/jbc.M708134200 ISSN 0021-9258.
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Official URL: http://dx.doi.org/10.1074/jbc.M708134200
Abstract
The Tat system transports folded proteins across bacterial and thylakoid membranes. In Gram-negative organisms, a TatABC substrate-binding complex and separate TatA complex are believed to coalesce to form an active translocon, with all three subunits essential for translocation. Most Gram-positive organisms lack a tatB gene, indicating major differences in organization and possible differences in mode of action. Here, we have studied Tat complexes encoded by the tatAdCd genes of Bacillus subtilis. Expression of tatAdCd in an Escherichia coli tat null mutant results in efficient export of a large, cofactor-containing E. coli Tat substrate, TorA. We show that the tatAd gene complements E. coli mutants lacking either tatAE or tatB, indicating a bifunctional role for this subunit in B. subtilis. Second, we have identified and characterized two distinct Tat complexes that are novel in key respects: a TatAdCd complex of similar to 230 kDa that is significantly smaller than the analogous E. coli TatABC complex (similar to 370 kDa on BN gels) and a separate TatAd complex. The latter is a discrete entity of similar to 270 kDa as judged by gel filtration chromatography, very different from the highly heterogeneous E. coli TatA complex that ranges in size from similar to 50 kDa to over 600 kDa. TatA heterogeneity has been linked to the varying size of Tat substrates being translocated, but the singular nature of the B. subtilis TatAd complex suggests that discrete TatAC and TatA complexes may form a single form of translocon.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH426 Genetics Q Science > QR Microbiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) |
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Library of Congress Subject Headings (LCSH): | Translocation (Genetics), Proteins -- Physiological transport, Gram-positive bacteria, Escherichia coli -- Genetics | ||||
Journal or Publication Title: | Journal of Biological Chemistry | ||||
Publisher: | American Society for Biochemistry and Molecular Biology | ||||
ISSN: | 0021-9258 | ||||
Official Date: | 1 February 2008 | ||||
Dates: |
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Volume: | Volume 283 | ||||
Number: | Number 5 | ||||
Number of Pages: | 9 | ||||
Page Range: | pp. 2534-2542 | ||||
DOI: | 10.1074/jbc.M708134200 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access | ||||
Funder: | Bacell Systems, European Union (EU), Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) | ||||
Grant number: | LSHC-CT2004-05257 (BS) |
Data sourced from Thomson Reuters' Web of Knowledge
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