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Molecular and Cellular Biology, May 2000, p. 3234-3244, Vol. 20, No. 9
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Cid1, a Fission Yeast Protein Required for S-M Checkpoint Control when DNA Polymerase delta  or epsilon  Is Inactivated

Shao-Win Wang,1 Takashi Toda,2 Robert MacCallum,3 Adrian L. Harris,1 and Chris Norbury1,*

Imperial Cancer Research Fund Molecular Oncology Laboratory, University of Oxford Institute of Molecular Medicine, John Radcliffe Hospital, Oxford OX3 9DS,1 and Imperial Cancer Research Fund Cell Regulation Laboratory2 and Biomolecular Modelling Laboratory,3 London WC2A 3PX, United Kingdom

Received 18 October 1999/Returned for modification 22 December 1999/Accepted 31 January 2000

The S-M checkpoint is an intracellular signaling pathway that ensures that mitosis is not initiated in cells undergoing DNA replication. We identified cid1, a novel fission yeast gene, through its ability when overexpressed to confer specific resistance to a combination of hydroxyurea, which inhibits DNA replication, and caffeine, which overrides the S-M checkpoint. Cid1 overexpression also partially suppressed the hydroxyurea sensitivity characteristic of DNA polymerase delta  mutants and mutants defective in the "checkpoint Rad" pathway. Cid1 is a member of a family of putative nucleotidyltransferases including budding yeast Trf4 and Trf5, and mutation of amino acid residues predicted to be essential for this activity resulted in loss of Cid1 function in vivo. Two additional Cid1-like proteins play similar but nonredundant checkpoint-signaling roles in fission yeast. Cells lacking Cid1 were found to be viable but specifically sensitive to the combination of hydroxyurea and caffeine and to be S-M checkpoint defective in the absence of Cds1. Genetic data suggest that Cid1 acts in association with Crb2/Rhp9 and through the checkpoint-signaling kinase Chk1 to inhibit unscheduled mitosis specifically when DNA polymerase delta  or varepsilon  is inhibited.

* Corresponding author. Mailing address: Imperial Cancer Research Fund Molecular Oncology Laboratory, University of Oxford Institute of Molecular Medicine, John Radcliffe Hospital, Oxford OX3 9DS, United Kingdom. Phone: 44 1865 222415. Fax: 44 1865 222431. E-mail: c.norbury{at}icrf.icnet.uk.

Molecular and Cellular Biology, May 2000, p. 3234-3244, Vol. 20, No. 9
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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