FIGURE 5.

MRB1 proteins interacting with MRB8170 and MRB4160. (A) The proteins identified by mass spectroscopy of the TAP purification of MRB8170 and MRB4160 described in Table 1 are depicted in the scheme introduced by Ammerman and colleagues (Ammerman et al. 2011). The names or gene tags of all proteins described from various MRB1 purifications (Ammerman et al. 2011) are enclosed in the large dashed oval, while the core MRB1 proteins are depicted in the small dotted oval. The proteins associated with either of the TAP-tagged MRB8170 and MRB4160 in the absence of RNase is enclosed by a thick dark line. Proteins that were demonstrated to have RNA-dependent or -enhanced interactions are with double and single underlines, respectively. (B) Immunoblot of TEV eluates from the first column of the TAP purification of MRB8170 and MRB4160, performed in the absence (−) and presence (+) of an RNase cocktail degrading both single- and double-stranded RNAs, The membrane was probed with antibodies recognizing MRB1 proteins GAP1, MRB3010, TbRGG2, and MRB8170. The band recognizing the endogenous and not the larger TAP-tagged MRB8170 protein is shown for this purification. An antibody recognizing the myc-epitope present in the TAP-tag was used as a loading control between the RNase-untreated and -treated purifications.