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Fig. 3. Sequence analysis of a U. maydis Wee1-like protein. (A) Schematic representation of the Wee1 protein in relation to other fungal Wee1-like proteins. The catalytic domains are shown in black and were identified using the Simple Modular Architecture Research Tool (http://smart.embl-heidelberg.de). The percentages inside each box represent the sequence identity when compared to the U. maydis sequence. (B) Dendrogram of Wee1-like proteins. The tree was reconstructed using the ClustalW method (http://www.ebi.ac.uk/clustalw/). Bar: 0.05 substitutions per aa. (C) Comparison of the catalytic domain of U. maydis Wee1 kinase with that of related Wee1-like proteins. The roman numerals indicate the catalytic subdomains as designated by Hanks (Hanks, 1991). The shaded residues are amino acids characteristic of Wee1 family kinases. (D) Protein levels at different stages of the cell cycle. Extracts from UMC38 cells carrying a myc-tagged copy of Wee1 and arrested at S or M phase, G1 phase enriched or cells growing asynchronously (As) were immunoblotted. The same filters were probed with anti-myc and anti-PSTAIRE antibodies and Cdk1 levels were used as loading controls. (E) Levels of wee1 expression at different cell cycle stages. RNA extracted from wild-type FB1 cells arrested at S phase or M phase, or enriched in G1 phase and growing asynchronously (As), was analyzed by northern blotting. The filter was hybridized with probes for wee1 and 18s rRNA as a control of loading.
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