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. 2013 Jan 9;449(Pt 3):673–681. doi: 10.1042/BJ20120952

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© 2013 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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(A) Schematic description of FL and truncated versions of Rfa2. Rfa2-FL (HT1 and HT2), Rfa2-CΔ182 (HT31 and HT33) containing residues 1–190 and Rfa2-NΔ40 (HT30 and HT32) containing residues 41–272 were expressed in WT or pph3Δ (SJL2) mutant cells. (B) Western blot analysis of Rfa2 extracted from WT (HT1, HT30 and HT31) and pph3Δ (HT2, HT32 and HT33) cells expressing different versions of Rfa2 in G₁-phase and after release. An anti-PSTAIRE antibody was used to detect Cdc28 as a loading control. (C) Western blot analysis of Rfa2 extracted from the same set of cells as above during G₁-phase and after HU treatment.