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. 2017 Dec 30;46(5):2321–2334. doi: 10.1093/nar/gkx1305

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© The Author(s) 2017. 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 6. — The core domain of Spn1 is competent for interaction with RNAPII, but is not stably recruited to the CYC1 promoter prior to activation of transcription. (A) Cell lysates prepared from the indicated strains were incubated with IgG sepharose beads. After extensive washing, TAP-tagged protein complexes were released from the beads by TEV protease cleavage. Protein extracts loaded onto the IgG sepharose (Input) and the released proteins (purified) were analyzed by immunoblotting with polyclonal anti-Spn1 and monoclonal anti-RNA Polymerase II (Covance 8WG16) antibodies. (B) ChIP analysis of Myc-tagged wild type Spn1 and Spn1^141–305 occupancy at the CYC1 promoter under repressive (glucose) and activating (ethanol) growth conditions. Occupancies were normalized to an un-tagged strain and then to the telomere proximal region.