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MBC in Press, published online ahead of print May 21, 2008
Mol. Biol. Cell 10.1091/mbc.E08-01-0057

A more recent version of this article appeared on July 1, 2008 Originally published as MBC in Press, 10.1091/mbc.E08-01-0057 on May 14, 2008
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Submitted on January 22, 2008
Revised on April 14, 2008
Accepted on May 1, 2008

Molecular and Genetic Analysis of Condensin Function in Vertebrate Cells

Damien F. Hudson,*{dagger}{ddagger} Shinya Ohta,* Tina Freisinger,*{sect} Fiona MacIsaac,* Lau Sennels,* Flavia Alves,* Fan Lai,*|| Alastair Kerr,* Juri Rappsilber,* and William C. Earnshaw*

*Wellcome Trust Centre for Cell Biology, Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom; {dagger}Murdoch Children’s Research Institute, Royal Children’s Hospital, Melbourne, Victoria 3052, Australia; {ddagger}Department of Paediatrics, University of Melbourne, Royal Children’s Hospital, Melbourne, Victoria 3052, Australia; {sect}Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany; ||{sect}Centre for Genomic Regulation, Parc de Recerca Biomèdica de Barcelona (PRBB), E-08003 Barcelona, Spain

Monitoring Editor: A. Gregory Matera

We engineered mutants into residues of SMC2 to dissect the role of ATPase function in the condensin complex. These residues are predicted to be involved in ATP binding or hydrolysis and in the Q-loop, which is thought to act as a mediator of conformational changes induced by substrate binding. All the engineered ATPase mutations resulted in lethality when introduced into SMC2 null cells. We found that ATP binding, but not hydrolysis, is essential to allow stable condensin association with chromosomes. How SMC proteins bind and interact with DNA is still a major question. Cohesin may form a ring structure that topologically encircles DNA. We examined if condensin behaves in an analogous way to its cohesin counterpart and have generated a cleavable form of biologically active condensin with PreScission protease sites engineered into the SMC2 protein. This has allowed us to demonstrate that topological integrity of the SMC2-SMC4 heterodimer is not necessary for the stability of the condensin complex in vitro or for its stable association with mitotic chromosomes. Thus, despite their similar molecular organization, condensin and cohesin exhibit fundamental differences in their structure and function.

Address correspondence to: Damien F. Hudson (Damien.Hudson{at}mcri.edu.au) or William C. Earnshaw (Bill.Earnshaw{at}ed.ac.uk)






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