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. 2017 Jan 23;45(8):4853–4865. doi: 10.1093/nar/gkw1361

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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 4. — Assembly factors that bind to domain V fail to associate with preribosomes in the erb1Δ161–200 and erb1Δ201–245 mutants. The protein composition of preribosomes purified from erb1 mutants using TAP-tagged AF Rpf2 (A) or Nop7 (B) as bait was assayed by SDS-PAGE, followed by silver staining. Western blotting was used to assay levels of select AFs and r-proteins in the preribosomes. (C) Relative changes in levels of large subunit AFs (mutant:WT) found in Rpf2-TAP particles were determined by semi-quantitative iTRAQ mass spectrometry. The ratios were normalized to levels of the bait protein, and the fold change of two biological replicates per mutant is present in log₂ scale.