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. 2008 Oct 6;183(1):87–99. doi: 10.1083/jcb.200803034

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© 2008 Wang et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 7. — GTP-dependent binding of preSSu to TOC translocons is mediated by atToc159. (A) Energy-depleted, in vitro–translated [³⁵S]preSSu was incubated with isolated chloroplasts from WT:ppi2 or A864R:ppi2 plants in the presence of 0.1 mM GTP to promote GTP-dependent binding. The homo-bifunctional cross-linker DTME was added to cross-link the bound preprotein to TOC components. After quenching the cross-linker, the chloroplasts were detergent solubilized and proteins immunoprecipitated with atToc159 or atToc33 affinity-purified antibodies or preimmune serum. The immunoprecipitates were analyzed by SDS-PAGE and phosphorimaging to quantify coimmunoprecipitated [³⁵S]preSSu or quantitative immunoblotting to detect atToc159 or atToc33. (B) Quantification of the levels of preSSu coimmunoprecipitating with atToc33 or atToc159 from WT:ppi2 or A864R:ppi2 chloroplasts. The quantification is from the single experiment presented in A. The data are representative of three replicate experiments.