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. 2010 Dec 1;21(23):4212–4226. doi: 10.1091/mbc.E10-04-0287

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© 2010 by The American Society for Cell Biology

This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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Figure 8. — RRP1B and PP1γ copurify an overlapping subset of pre-60S ribosomal subunit processing proteins. (A) An overlay of mammalian orthologues on their yeast counterparts in a yeast-derived map of pre-60S ribosomal subunit processing proteins demonstrates a specific enrichment of midlate processing complexes. Of the 72 proteins predicted in the yeast map, 66 have known mammalian orthologues. Of these, 49 (74%) were found in both the RRP1B and PP1γ interactomes (yellow), with an additional eight proteins only detected with the phosphatase (green). This may represent different subcomplexes or a difference in sensitivity of the experiment. Of the nine proteins that were not enriched (gray), most are peripheral to the core complex and function later in the processing/export pathway. In addition to these nonribosomal processing proteins, 36/40 (90%) of 60S subunit RPL proteins were specifically enriched with RRP1B and PP1γ. (B) 60S processing proteins identified in a recent nonquantitative screen of TAP-tagged yeast Rrp1p are indicated in this table, which includes both the yeast and mammalian gene names for each protein and uses the same color coding as in A to indicate whether a protein was found in our RRP1B and/or PP1γ IP or neither.