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8. Roc2 and Cul5 are exclusive binding partners. A, Extracts were prepared from embryos with either a wild-type (Gen = +) or Roc2 mutant (Gen = Roc2KG) background and the indicated transgene. The immunoprecipitated FLAG-Roc protein is indicated at the top. (2) indicates no transgene. doi:10.1371/journal.pone.0002918.gdomain that is more similar between Roc1a and Roc1b than Roc2 participates in Ro
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
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
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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