Combining gene expression data with EWS-FLI1 binding, we observed that proximal and distal binding of EWS-FLI1 were both associated with higher RNA levels, suggesting that EWS-FLI1 acts as a transcriptional activator not only when it binds in direct vicinity to the TSS but also at enhancers outside of the promoter region.
Consistent with the data on CTCF binding, we observed that the insulator activity of IC1 is modestly affected by the 2.2 kb (B5/B1) deletion but severely reduced by the 1.4 kb (B5/B3) and 1.8 kb (both B5/B2 and B6/B3) deletions.
These results are in sharp contrast to what we observed; the precise overlap produces enhanced GABPα and CREB binding, suggesting that the cooperative binding we observed between the ETS and CREB DNA binding domains is distinct from the cooperative binding observed when full-length proteins are examined.
We observe that ligand binding at each site alters the structure and dynamics of NS5B in a distinct manner.
On the other hand, in the same binding experiment, we observed that the smaller 80 kDa PfRH2a/b fragment exhibited a different erythrocyte binding phenotype (Figures 3A and S6B).
In our effort to determining the protein subunit(s) responsible for H3 tail binding activity, we observed that the CHD3, MTA family proteins and RbAp48 all exhibited a H3 tail peptide binding specificity resembling to that of NURD.
In agreement with previous reports, indicating that Sec61p displays the majority of the ER ribosome binding activity, we observed that Sec61p is shielded from proteolytic digestion by native, bound ribosomes.
We hypothesize that the binding we observe is a reflection of the molar excess of the amplified material available for binding.
However, when a mixture containing comparable amount of unsumoylated and monosumoylated DRIL1 (Fig. 5B, lane 4) was assayed for binding to E2F1, we observed that E2F1 preferentially interacts with unsumoylated DRIL1 (Fig. 5B, lane 5).
Moreover, in agreement with the notion that the ability of SGK3 to be inhibited by VPS34-IN1 is dependent on its PtdIns(3) P-binding PX domain, we observed that VPS34-IN1 did not inhibit the activity of SGK2 isoform that does not possess a PX domain.
Upon examination of probes contributing to overrepresentation of GO-terms; "cytosolic large and small ribosomal subunits", "protein biosynthesis", "ribosome", "structural constituent of ribosome", "RNA-binding" and "intracellular", we observed that 18 probes, representing transcripts encoding 15 ribosomal proteins were largely responsible for enrichment of these GO-terms.
