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. 2020 Nov 10;48(21):12116–12134. doi: 10.1093/nar/gkaa1003

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© The Author(s) 2020. 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 Non-Commercial 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 5. — LSH specifically interacts with UHRF1. (A) Western blots showing reciprocal co-IP of endogenous LSH and UHRF1 in HeLa cell extracts. Note DNMT3A, DNMT3B and DNMT1 were not detected in IP of LSH, whereas DNMT1 was detected in IP of UHRF1. (B) Western blots showing ectopically expressed FLAG-LSH co-immunoprecipitated with endogenous UHRF1 but not DNMT3A, DNMT3B and DNMT1. (C) Western blots showing co-IP of ectopically expressed HA-UHRF1 and FLAG-LSH. (D) Western blots showing co-IP of ectopically expressed FLAG-LSH with HA-UHRF1 but not HA-DNMT1. (E) In vitro GST pulldown assay showing purified FLAG-LSH bound to recombinant GST-UHRF1 but not control GST proteins. (F) Western blots showing knockout of LSH did not affect the interaction between UHRF1 and DNMT1. (G) Schematic illustration of UHRF1 structural and functional domains. (H) Western blots showing deletion of UBL domain impaired interaction between UHRF1 and LSH. (I) Western blots showing the UBL domain is not sufficient for interaction with LSH.