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G to Cullin protein [26] and forms a b-strand that makes an inter-molecular b-sheet with the Cullin protein [11,14]. Our analysis of ``RING swap'' protein chimeras indicates that in some instances the Roc NH2-terminal b-strand is the primary contributor to Roc-Cullin binding specificity. Both fusing the Roc2 NH2 terminus to the Roc1a RING domain (2NAR) and fusing the Roc1a NHterminus to Rob1b (AN
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A promoter. If the NH2-terminus is sufficient to confer Cullin binding specificity, all chimeras with the same NH2-terminal Roc sequence should bind the same Cullins, regardless of the RING domain to which they are fused. We transfected these constructs into S2 cells and determined Cullin binding by IP/immunoblot. Because we had already observed that Roc1a binds Cul1 and Cul3 but not Cul5, thatRo
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Mains of TRAF3 and TRAF5 is also incapable of NF-kB activation. The authors proposed that these chimeric proteins might not be able to chelate zinc ions or fold properly. This may explain why AN2R is unable to bind any Cullin. However, the other Roc chimeras we constructed were able to bind Cullin and were active as E3 ligases. Moreover, the rescue of male sterility by the ANBR chimera (see below
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