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. 2008 May 3;36(11):3579–3589. doi: 10.1093/nar/gkn236

Figure 2.

Figure 2.

Nitrocellulose filter-binding assays between truncated Tudor-SN mutants and RNA. (A) The binding assays show that TSN, TSN-90, TSN-70 and TSN64 all bind the 20-bp IIUI-dsRNA with comparable affinity, whereas TSN-50 and TSN-25 cannot bind RNA. (B) The filter-binding assays between Tudor-SN proteins and the 20-bp AAUA-dsRNA show that the truncated proteins containing more tandem repeats of SN domains bind AAUA-dsRNA better. TSN-50 and TSN-25 did not bind AAUA-dsRNA. (C) SDS–PAGE analysis of purified TSN-SN34. (D) The filter binding assays between TSN-SN34 and RNA. (E) The summary of the apparent dissociation constants (Kdapp) between Tudor-SN proteins and 20-bp IIUI- and AAUA-dsRNAs.