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. 2006 Oct 9;103(42):15588–15593. doi: 10.1073/pnas.0604524103

Fig. 3.

Fig. 3.

HMM A3G complexes correspond to at least three RNP complexes. (A) NTAP-tagged Staufen1 (Stau), a 55-kDa splicing variant of Staufen1 (Stau55), and 60-kDa Ro were subjected to TAP after expression in the absence or presence of HA–A3G coexpression. As controls, cell lysates containing unlinked NTAP and HA–A3G were identically processed (lanes 1 and 7). Arrow, HA–A3G copurified with NTAP–Ro; arrowheads, nucleolin and 50-kDa La. (B) Purified proteins were immunoblotted with antibodies reacting with the indicated proteins. Association of HA–A3G with NTAP–Stau (Stau55) and NTAP–Ro RNPs was detected by anti-HA (top sets of panels). (C) Endogenous A3G associates with the same RNP complexes. Lysates from A3G-expressing H9 T cells were subjected to IP with antibodies reacting with p68 helicase, a major component of RNA-transporting granules, and 60-kDa Ro, a major component of Ro RNPs, followed by immunoblotting. IP with protein G-agarose was included as a negative control.