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. 2014 May 16;5:203. doi: 10.3389/fpls.2014.00203

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Copyright © 2014 Hardré, Kuhn, Albrieux, Jouhet, Michaud, Seigneurin-Berny, Falconet, Block and Maréchal.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Topological information possibly provided by the tag and shave strategy, coupled with 2D-PAGE proteomic analyses. Chloroplasts isolated from leaves are either superficially tagged with biotin (A), superficially shaved by proteolysis with thermolysin (C) or untreated (B). (A) Outer envelope membrane (OEM) proteins that are possibly biotinylated are detected after biotin detection (proteins 1, 2, and 8), whereas OEM proteins that fail to be biotinylated are not tagged under these conditions (protein 3). Internal proteins (proteins 4, 5, 6, and 7) are not tagged. (C) Outer envelope membrane proteins that are possibly degraded by thermolysin disappear from the 2D-PAGE gel (proteins 2, 3, and 8, indicated by crosses), whereas OEM proteins that fail to be degraded are not shaved under these conditions (protein 1). Internal proteins are theoretically not shaved. However, internal proteins (such as protein 6) that bind to the IEM depending on the integrity of OEM proteins (stable trans-envelope complex, such as 6-7-8), will dissociate form the envelope after thermolysin treatment (protein 6, indicated by an arrow).