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Individual SCF Pop1pand SCF Pop2pcomplexes bearing ubiquitin ligase activity
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.
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.
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.
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.