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Vol. 10, Issue 10, 3223-3238, October 1999

Requirement of Sequences outside the Conserved Kinase Domain of Fission Yeast Rad3p for Checkpoint Control

Carolyn Riley Chapman,^* Sarah Tyler Evans,^* Antony M. Carr, and Tamar Enoch^*§

 ^*Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115; and  Medical Research Council Cell Mutation, Sussex University, Falmer, Brighton, BN1 9RR, United Kingdom

The fission yeast Rad3p checkpoint protein is a member of the phosphatidylinositol 3-kinase-related family of protein kinases, which includes human ATMp. Mutation of the ATM gene is responsible for the disease ataxia-telangiectasia. The kinase domain of Rad3p has previously been shown to be essential for function. Here, we show that although this domain is necessary, it is not sufficient, because the isolated kinase domain does not have kinase activity in vitro and cannot complement a rad3 deletion strain. Using dominant negative alleles of rad3, we have identified two sites N-terminal to the conserved kinase domain that are essential for Rad3p function. One of these sites is the putative leucine zipper, which is conserved in other phosphatidylinositol 3-kinase-related family members. The other is a novel motif, which may also mediate Rad3p protein-protein interactions.

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   These authors contributed equally to this work.
^§   Corresponding author. E-mail address: enoch{at}rascal.med.harvard.edu.

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Molecular Biology of the Cell
Vol. 10, 3223-3238, October 1999
Copyright © 1999 by The American Society for Cell Biology

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