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While these data support the existence of distinct SCF Pop1pand SCF Pop2pcomplexes, individual binding of Pop1p and Pop2p to SCF core components in the absence of their heterodimerizing F-box protein partners does not rule out the possibility that these complexes represent inactive intermediates formed during the normal assembly of functional SCF Pop1p-Pop2pcomplexes.
In the wild type lenses, typical cross-sectional patterns of fiber cells organized in radial columns were observed (Figure 3K,3N,3Pand 3S).
These data indicate that Pop1p and Pop2p assume their subcellular localization pattern independent of each other, indicating the possibility of distinct nuclear and cytoplasmic homooligomeric SCF Pop1pand SCF Pop2pcomplexes.
Since the substrates of putative SCF Pop1pand SCF Pop2pubiquitin ligases are unknown, we adopted a substrate-independent assay originally described by Lyapina et al . [ 27 ] . For this experiment, we again used the strains harboring genomically integrated Myc epitope-tagged Pop1p or Pop2p in a background deficient in the respective heterooligomerization partner ( Δpop2 pop1-13myc , Δpop1 pop2-13myc strains).
To exclude this possibility, we asked whether distinct SCF Pop1pand SCF Pop2pcomplexes bear ubiquitin ligase activity in vitro . To this end, we performed in vitro ubiquitylation assays.