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. 2014 Dec 8;43(1):336–347. doi: 10.1093/nar/gku1232

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© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 8. — NC domain binds Tsg101 in vitro. GST, GST-p6, GST-p7^NC, GST-p9^NCp1, GST- p9^NCΔZF2p1 or GST-p15^NCp1p6 fusion protein was expressed in E. coli, captured on glutathione-conjugated beads, and subsequently incubated with lysates from 293T cells naturally expressing Tsg101 but transfected to produce non-coding HIV gRNA. Captured proteins and cell lysates were analyzed by SDS-PAGE and western blotting using an anti-Tsg101 antibody. GST fusion proteins in pulldown samples were visualized by Coomassie blue staining. (A) Tsg101 interaction with p7 or p9 fusion proteins. (B) Effect of the ZF2 deletion in the p9-Tsg101 interaction. (C) Comparative analysis of p15 and p6 ability to bind Tsg101.