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Molecular and Cellular Biology, June 2006, p. 4690-4700, Vol. 26, No. 12
0270-7306/06/$08.00+0 doi:10.1128/MCB.02315-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109,1 Molecular and Cellular Biology Program, University of Washington, Seattle, Washington 98195,2 The Institute for Genomic Research, Rockville, Maryland 20850,3 Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan4
Received 4 December 2005/ Returned for modification 4 January 2006/ Accepted 13 April 2006
The macronucleus of the binucleate ciliate Tetrahymena thermophila contains fragmented and amplified chromosomes that do not have centromeres, eliminating the possibility of mitotic nuclear division. Instead, the macronucleus divides by amitosis with random segregation of these chromosomes without detectable chromatin condensation. This amitotic division provides a special opportunity for studying the roles of mitotic proteins in segregating acentric chromatin. The Smc4 protein is a core component of the condensin complex that plays a role in chromatin condensation and has also been associated with nucleolar segregation, DNA repair, and maintenance of the chromatin scaffold. Mutants of Tetrahymena SMC4 have remarkable characteristics during amitosis. They do not form microtubules inside the macronucleus as normal cells do, and there is little or no bulk DNA segregation during cell division. Nevertheless, segregation of nucleoli to daughter cells still occurs, indicating the independence of this process and bulk DNA segregation in ciliate amitosis.
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