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Eukaryotic Cell, October 2003, p. 910-921, Vol. 2, No. 5
1535-9778/03/$08.00+0 DOI: 10.1128/EC.2.5.910-921.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.
Dynamique du Genome, URA 1644 du CNRS, Institut Pasteur, 75724 Paris, Cedex 15, France,1 Institute of Interdisciplinary Research (IRIBHN), School of Medicine, University of Brussels, B1070 Brussels, Belgium2
Received 31 March 2003/ Accepted 8 July 2003
Sap1 is a dimeric sequence-specific DNA binding-protein, initially identified for its role in mating-type switching of the fission yeast Schizosaccharomyces pombe. The protein is relatively abundant, around 10,000 dimers/cell, and is localized in the nucleus. sap1+ is essential for viability, and transient overexpression is accompanied by rapid cell death, without an apparent checkpoint response and independently of mating-type switching. Time lapse video microscopy of living cells revealed that the loss of viability is accompanied by abnormal mitosis and chromosome fragmentation. Overexpression of the C terminus of Sap1 induces minichromosome loss associated with the "cut" phenotype (uncoupling mitosis and cytokinesis). These phenotypes are favored when the C terminus of Sap1 is overexpressed during DNA replication. Fluorescence in situ hybridization experiments demonstrated that the cut phenotype is related to precocious centromere separation, a typical marker for loss of cohesion. We propose that Sap1 is an architectural chromatin-associated protein, required for chromosome organization.
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