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. 2016 Oct 11;13(12):1274–1285. doi: 10.1080/15476286.2016.1239689

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© 2016 The Author(s). Published with license by Taylor & Francis Group, LLC

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 5. — The CAB box function is not required for AluACA7 accumulation. (A) RNase mappings. The dm1, dm2 and dm3 CAB box mutations introduced into the proximal and distal CAB (pCAB and dCAB) sequences of AluACA7 and AluACA17 and their predicted consequences on the BIO motif structure are shown. For other details, see the legends to Fig. 3. (B) Wdr79 fails to interact with AluACA7-dm2. Wdr79 was immunoprecipitated with a specific antibody (α-Wdr79) from total extracts (Ext) prepared from HeLa cells transiently overexpressing AluACA7 or AluACA7-dm2 as indicated above the lanes. Co-IP of AluACA7 and AluACA7-dm2 was monitored by RNase mappings. Interaction of Wdr79 with the endogenous U85 H/ACA scaRNA (positive control) and the U64 snoRNA (negative control) was also tested. Recovery of Wdr79 was confirmed by western blot analysis. Lane no Ab, control IP performed without antibody.