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Notes: Fig. 1.B. shows that rdr2-1 mutants lacking RDR2 do not accumulate any of the endogenous siRNA tested (siRNA02, AtSN1 siRNA, Cluster2 siRNA, or siRNA1003).

Notes: Fig. 8 shows significant differences in TuMV-GFP–derived siRNA accumulation among the mutants; accumulation of siRNAs derived from the cylindrical inclusion (CI) or from the 5′ UTR of TuMV was significantly reduced in each single, double, and triple mutants with the rdr1-1 allele. This suggests that RDR1 is a major contributor to biogenesis of TuMV-derived siRNAs.

Supplemental Fig. 5.B. shows that ago7 mutants lacking AGO7 have a modest increase in ΔCP and TCV-GFP RNA accumulation. This suggests that AGO7 may not be the most efficient slicer of RNA, but serves as a surrogate slicer in the absence of AGO1.

Fig. 1.B. and 1.C. show that drb4 mutants lacking DRB4 have enhanced severity of virus infection symptoms. Viral coat protein levels are higher in drb4 mutants and dcl4 mutants compared to wildtype.

However, Fig. 3. shows that viral RNA levels are not elevated (unlike in dcl4 mutants), suggesting that DRB4 does not act in viral gene silencing.

Supplemental Figure S5. shows that ago1-11 mutants (which have partial loss of AGO1 function) have higher levels of ΔCP RNA accumulation than wild-type when infected with a turnip crinkle virus (TCV) mutant without a silencing suppressor.

Figure 5.A. (right) shows that only mutants lacking DCL4 (dcl4, dcl2/dcl4, dcl3/dcl4, and dcl2/dcl3/dcl4), when infected with TuMV-AS9-GFP (which lacks a silencing suppressor), have infection levels comparable to when infected with TuMV-GFP.

Fig. 1C shows that AtRAR1 (RAR1 from Arabidopsis) interacts with AtSGT1a and AtSGT1b (SGT1a and SGT1b from Arabidopsis, respectively) using a yeast two-hybrid screen of Arabidopsis.

Fig. 1B shows that both HvRAR1 (RAR1 from barley) and AtRAR1 (RAR1 from Arabidopsis) interact with HvHSP90 (HSP90 from barley); the HSP90-binding function is likely conserved between monocots and dicots.

The first paragraph of the Results section ("RAR1 Interacts with HSP90") mentions how the authors found using a yeast two-hybrid screen of Arabidopsis that Arabidopsis HSP90.1 (AtHSP90.1) also interacts with RAR1 (data not shown).

Fig. 2A shows the protein is present in the total and microsomal membrane fractions, but not in the soluble fraction; the protein is likely associated with the membrane.

Fig. 2B shows that treatments with detergent (to solubilize the microsomal membrane), sodium carbonate or urea (which do little damage to the lipid bilayer), and even extraction buffer (due to the physical force of resuspension) can release the protein from the membrane; the protein is likely not transmembrane.

Fig. 2D shows that RPM1∷MYC, like RD28, is enriched in the plasma membrane vesicles; the protein is likely associated with the plasma membrane.