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ATP-Induced Shrinkage of DNA with MukB Protein and the MukBEF Complex of Escherichia coli

Department of Physics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan,¹ Spatio-Temporal Order Project, ICORP, JST, Kyoto University, Kyoto, Japan,² Graduate School of Environmental Studies, Nagoya University, Nagoya 464-8601, Japan,³ Faculty of Education for Future Generations, International Pacific University, Okayama 709-0863, Japan,⁴ Department of Radiation Genetics, Graduate School of Medicine, 606-8502, Kyoto University, Kyoto, Japan,⁵ Radiation Laboratory Center, Wakayama Medical University, School of Medicine, 811-1, Kimiidera, Wakayama 641-8509, Japan⁶

Received 27 November 2007/ Accepted 3 March 2008

Fluorescence microscopic observation of individual T4 DNA molecules revealed that the MukBEF complex (bacterial condensin) and its subunit, the MukB (a member of the SMC [structural maintenance of chromosomes] superfamily) homodimer, of Escherichia coli markedly shrunk large DNA molecules in the presence of hydrolyzable ATP. In contrast, in the presence of ADP or ATP-S, the conformation of DNA was almost not changed. This suggests that the ATPase activity of subunit MukB is essential for shrinking large DNA molecules. Stretching experiments on the shrunken DNA molecules in the presence of ATP and MukBEF indicated a cross-bridging interaction between DNA molecules.

Published ahead of print on 7 March 2008.