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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 A., 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, Vol.70 (No.1). pp. 140-150. ISSN 0950-382X

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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
Subjects: Q Science > QD Chemistry
Q Science > QR Microbiology
Divisions: Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Faculty of Science > Mathematics
Journal or Publication Title: Molecular Microbiology
Publisher: Wiley-Blackwell Publishing Ltd.
ISSN: 0950-382X
Date: October 2008
Volume: Vol.70
Number: No.1
Number of Pages: 11
Page Range: pp. 140-150
Identification Number: 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
URI: http://wrap.warwick.ac.uk/id/eprint/29365

Data sourced from Thomson Reuters' Web of Knowledge

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