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(Received for publication, December 13, 1996, and in revised form, February 14, 1997)
From the Departments of Molecular Biology and Cell Biology, The
Scripps Research Institute, La Jolla, California 92037
Wee1 tyrosine kinase regulates mitosis by
carrying out the inhibitory tyrosine 15 phosphorylation of Cdc2 M-phase
inducing kinase. Schizosaccharomyces pombe Wee1 is a large
protein, consisting of a C-terminal catalytic domain of ~350 amino
acids preceded by a N-terminal domain of ~550 residues. The
functional properties of the Wee1 N-terminal domain were investigated
by expressing truncated forms of Wee1 in S. pombe. Both
positive and negative regulatory domains were identified. Sequences
important for Wee1 function were mapped to a central region (residues
363-408). This region is not required for kinase activity or nuclear
localization, suggesting it may be involved in substrate recognition.
The negative regulatory domain resides in the N-terminal third of Wee1,
Wee1 constructs lacking this domain are more effective at delaying mitosis than wild-type Wee1. The negative regulatory domain contains clusters of potential Cdc2 phosphorylation sites. Investigations to
monitor the abundance of Wee1 mRNA and protein during the cell cycle were also carried out.
Volume 272, Number 20,
Issue of May 16, 1997
pp. 13320-13325
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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