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. 2020 Apr 27;48(10):5397–5406. doi: 10.1093/nar/gkaa290

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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 License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Ocr interacts with the methyltransferase BrxX. A 4–20% gradient SDS gel showing the results of pull-downs from extracts of E. coli EcoKI R–M+ strain BW25113 expressing, from compatible plasmids, Ocr (with or without a Strep-tag) and BREX (with or without Strep- tags on BrxX or BrxZ). Lane 1: Ocr-Strep pulled down from BREX- cells; lane 2: Ocr-Strep pulled down from BREX+ cells; lane 3: BrxX-Strep pulled down from BREX+ cells producing Ocr; lane 4: BrxZ-Strep pulled down from BREX+ cells producing Ocr; lane 5: BrxX-Strep pulled down from cells infected with wild-type T7 at MOI = 1; lane 6: BrxZ-Strep pulled down from cells infected with wild-type T7 at MOI = 1; M: PageRuler Prestained Plus ladder. Tagged proteins are labelled with an asterisk. Proteins DnaK and AccB were detected in all tested samples and thus must be non-specifically binding to the affinity resin and/or overexpressed proteins.