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Tat-dependent targeting of Rieske iron-sulphur proteins to both the plasma and thylakoid membranes in the cyanobacterium Synechocystis PCC6803
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Aldridge, Cassie, Spence, Edward M., Kirkilionis, Markus, Frigerio, Lorenzo and Robinson, Colin (2008) Tat-dependent targeting of Rieske iron-sulphur proteins to both the plasma and thylakoid membranes in the cyanobacterium Synechocystis PCC6803. Molecular Microbiology, Volume 70 (Number 1). pp. 140-150. doi:10.1111/j.1365-2958.2008.06401.x
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Official URL: http://dx.doi.org/10.1111/j.1365-2958.2008.06401.x
Abstract
Cyanobacteria possess a differentiated membrane system and transport proteins into both the periplasm and thylakoid lumen. We have used green fluorescent protein (GFP)-tagged constructs to study the Tat protein transporter and Rieske Tat substrates in Synechocystis PCC6803. The Tat system has been shown to operate in the plasma membrane; we show here that it is also relatively abundant in the thylakoid membrane network, indicating that newly synthesized Tat substrates are targeted to both membrane systems. Synechocystis contains three Rieske iron-sulphur proteins, all of which contain typical twin-arginine signal-like sequences at their N-termini. We show that two of these proteins (PetC1 and PetC2) are obligate Tat substrates when expressed in Escherichia coli. The Rieske proteins exhibit differential localization in Synechocystis 6803; PetC1 and PetC2 are located in the thylakoid membrane, while PetC3 is primarily targeted to the plasma membrane. The combined data show that Tat substrates are directed with high precision to both membrane systems in this cyanobacterium, raising the question of how, and when, intracellular sorting to the correct membrane is achieved.
| Item Type: | Journal Article | ||||
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| Subjects: | Q Science > QP Physiology Q Science > QR Microbiology |
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| Divisions: | Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010) Faculty of Science > Mathematics |
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| Library of Congress Subject Headings (LCSH): | Cyanobacteria, Iron-sulfur proteins, Escherichia coli, Cell membranes, Proteins -- Physiological transport | ||||
| Journal or Publication Title: | Molecular Microbiology | ||||
| Publisher: | Wiley-Blackwell Publishing Ltd. | ||||
| ISSN: | 0950-382X | ||||
| Official Date: | October 2008 | ||||
| Dates: |
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| Volume: | Volume 70 | ||||
| Number: | Number 1 | ||||
| Number of Pages: | 11 | ||||
| Page Range: | pp. 140-150 | ||||
| DOI: | 10.1111/j.1365-2958.2008.06401.x | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access | ||||
| Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC) | ||||
| Grant number: | BB/C00437X (BBSRC) |
Data sourced from Thomson Reuters' Web of Knowledge
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