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. 2012 Aug 20;198(4):529–544. doi: 10.1083/jcb.201201153

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© 2012 Castilla-Llorente et al.

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Figure 7. — GW220 provides partial protection to a tethered mRNA target. (A) Schematic representation of the λN/boxB FLAG–β-globin–tethering reporter system. (B) The λN-HA–tagged C-terminal silencing domain of GW, GWSD(1,491C), localized in the nucleus and cytoplasm, whereas the λN-HA–tagged GW220 formed GW/P bodies in HeLa Tet-OFF cells. Tethering of GWSD(1,491C) led to significant mRNA destabilization that correlated well with protein repression. Tethering of GW220 caused less mRNA destabilization even though the protein was equally well repressed as tethering of GWSD(1,491C). (C) The λN-HA–tagged GW195 and GW182 formed cytoplasmic aggregates that were distinct from the GW/P bodies in the HeLa Tet-OFF cells. Tethering of GW195 and GW182 led to mRNA destabilization that correlated well with protein repression. The protein repression and mRNA destabilization were quantified by ImageJ software and Quantity One 1-D Analysis Software and confirmed by qRT-PCR analysis. GAPDH, glyceraldehyde 3-phosphate dehydrogenase. Mean values ± standard deviations from three independent experiments are shown. Bars, 10 µm.