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. 1999 Dec 27;147(7):1443–1456. doi: 10.1083/jcb.147.7.1443

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© 1999 The Rockefeller University Press

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.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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In export-deficient sec61 mutant microsomes, misfolded secretory proteins remain associated with PDI. Radiolabeled pΔgpαf was translocated into SEC61 wild-type and mutant microsomes as described in Materials and Methods and cross-linked with DSP. PDI– and BiP–cross-linked proteins were immunoprecipitated with the respective antibodies. Cross-links were cleaved with DTT, proteins resolved on 18% polyacrylamide gels containing 4 M urea, and radiolabeled Δgpαf associated with PDI or BiP was visualized by autoradiography and quantified using a PhosphorImager. Relative amounts of Δgpαf associated with PDI and BiP are indicated with and without adjustment for increased levels of BiP and PDI due to the unfolded protein response induction in the sec61 mutant microsomes (1.7× for sec61-32; 1.4× for sec61-41).