Figure 1.

(A) Comparison of the number of misregulated probe sets in the lss mutant versus the sunn-1 mutant. Data was obtained as in reference ⁷, except that data was normalized across ten independent experiments. DCHIP VERSION 1.3 (www.dchip.org) was used for primary data analyses. Data sets were filtered to eliminate probe sets with intensity values below 100 in both lines being compared and those with an absolute difference in intensity between the two lines of less than 100. Significantly different probe sets were then defined as those with an absolute difference of greater than two-fold and an absolute lower bound cutoff of 1.5. (B) Ribbon diagram of the predicted structure of the catalytic core of the Sunn kinase domain. Shown are the small N-terminal nucleotide binding lobe (yellow), the large C-terminal lobe (purple) and the predicted substrate binding pocket (red). The side chains of Glu857 and Arg950, forming a predicted ion pair between the substrate binding pocket and conserved kinase subdomain XI, are shown in blue. The sunn-1 allele has an R950K missense mutation that is predicted to disrupt the ion pair (see the text). The structure of the SUNN kinase domain was predicted by homology modeling using HHpred and MODELLER (Bioinformatics Toolkit, Max-Plank Institute for Developmental Biology, toolkit.tuebingen.mpg.de/) and visualized using DS ViewerPro 5.0 (www.accelrys.com).⁸,⁹