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. 2010 Mar 24;38(13):4231–4245. doi: 10.1093/nar/gkq162

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Domain-swapping experiment simulation. (A) Pairwise alignment of WG/GW-rich domains from Arabidopsis largest polV subunit, NRPE1 and Human GW182. (B) Outline of the virtual domain swapping experiment between plant and mammalian WG/GW proteins. Dos/ics score tables were calculated based on experimentally-verified plant/mammalian WG/GW proteins and subsequently used to search for WG/GW domains in mammalian/plant proteomes. Detected putative WG/GW motif proteins were compared with experimentally verified AGO-binding proteins. Reciprocal best protein hits of such a bidirectional procedure share a conserved amino-acid composition of WG/GW-rich AGO-binding sites.