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. 2010 Nov 1;21(21):3722–3734. doi: 10.1091/mbc.E10-08-0693

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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 9. — Rlg1 proteins interact with polysomes irrespective of existence of HAC1 mRNAs. (A) FLAG-AtRlg1p and FLAG-ScRlg1p were immunoprecipitated with anti-FLAG M2 agarose and eluted from the resin by incubating with a 3×FLAG peptide. The eluates were loaded onto a 16/50% step sucrose density gradient as in Figure 7B. (B–E) Extracts were prepared from HA-ScRLG1 HAC1 (B), HA-ScRLG1 hac1Δ (C), HA-AtRLG1[M74] HAC1 (D), and HA-AtRLG1[M74] hac1Δ (E) and sedimented through a 10–50% sucrose density gradient as in Figure 4. The fractions were subjected to Western blotting with an anti-HA antibody. In F and G, wild-type (W303-1A) and hac1Δ (TMSC09) strains with the authentic RLG1 on their chromosome were analyzed as above, and ScRlg1p in the fractions was detected with anti-Rlg1p antibodies. L, cell extract.