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These findings indicate the existence of distinct SCF Pop1pand SCF Pop2pcomplexes in vivo .
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).
In addition, compartmentalization of homooligomeric SCF Pop1pand SCF Pop2pcomplexes may direct the ubiquitylation of unknown nuclear and cytoplasmic substrates.
In addition, based on overexpression, distinct SCF Pop1pand SCF Pop2pcomplexes were proposed to target unknown substrates, but no biochemical evidence of their activity was provided [ 18 ] . To address these questions, we cloned two additional subunits of SCF Popand performed a detailed characterization of its activity in vitro and in vivo . Our results indicate that heterooligomeric SCF Pop1p-Pop2pmediates Rum1p ubiquitylation whereas distinct SCF Pop1pand SCF Pop2pcomplexes target unknown nuclear and cytoplasmic substrates, thereby generating combinatorial diversity of SCF function in fission yeast.
In the wild type lenses, typical cross-sectional patterns of fiber cells organized in radial columns were observed (Figure 3K,3N,3Pand 3S).