Your friend is intrigued by Cdks and purifies Cdk from the daisy plant. She is able to determine the sequence of 18 amino acids from the daisy Cdk protein. Using these data, she aligns the daisy Cdk sequence with one human Cdk protein and the Cdk proteins from two different kinds of yeast, as shown in Figure 18-25. Sequences identical between the human and fungal proteins have been boxed. ...FGIPIRVY THEVVTLWYR human S. pombe S. cerevisiae daisy ...FGVPLRNYTHEIVTLWYR... ... ... FGVPLRAY THEIVTLWYR. ...FGAPIKMYTHKIVTLWYR... #1 #2 Figure 18-25 Such conserved amino acid sequences are often involved in protein-protein interactions. Indeed, the threonine (T) in the central "YTHE" block is known to be phosphorylated by a kinase that activates Cdks in human and yeast. The surrounding conserved sequences could thus be important for the interaction of this Cdk-activating kinase with Cdk. In the daisy Cdk, however, not all of the amino acids in these conserved blocks match the sequences from yeast and human, as indicated by the arrows marked #1 and #2. A. When you replace the S. cerevisiae (budding yeast) Cdk with the daisy Cdk, you discover the daisy Cdk does not interact with the Cdk-activating kinase inside the yeast cell. Which of the changes (#1 or #2) is a conservative mutation? Which is non-conserved? Explain your reasoning (hint remember the biochemical properties of R groups!!). B. Circle the amino acid in the daisy Cdk that is likely to be the most disruptive to its interaction with Cdk-activating kinase. C. Based on the information in Figure 18-25 and what you know about the Cdk1-Cdk-activating kinase interaction, would you predict that the human Cdk will interact with yeast Cdk-activating kinase? Explain your reasoning.

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