한빛사 논문
Young-Min Soh1, Iain Finley Davidson2, Stefano Zamuner3, Jérôme Basquin4, Florian Patrick Bock1, Michael Taschner1, Jan-Willem Veening1, Paolo De Los Rios3, Jan-Michael Peters2, Stephan Gruber1,*
1 Department of Fundamental Microbiology (DMF), Faculty of Biology and Medicine (FBM), University of Lausanne (UNIL), Lausanne, Switzerland.
2 Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC) and Medical University of Vienna, Vienna, Austria.
3 Laboratory of Statistical Biophysics, Institute of Physics, School of Basic Sciences and Institute of Bioengineering, School of Life Sciences, École Polytechnique Féderale de Lausanne (EPFL), Lausanne, Switzerland.
4 Structural Cell Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.
*Corresponding author : Stephan Gruber
Abstract
ParABS systems facilitate chromosome segregation and plasmid partitioning in bacteria and archaea. ParB protein binds centromeric parS DNA sequences and spreads to flanking DNA. We show that ParB is an enzyme that hydrolyzes cytidine triphosphate (CTP) to diphosphate (CDP). parS DNA stimulates cooperative CTP binding by ParB and CTP hydrolysis. A nucleotide co-crystal structure elucidates the catalytic center of the dimerization-dependent ParB CTPase. Single-molecule imaging and biochemical assays recapitulate features of ParB spreading from parS in the presence but not absence of CTP. The findings suggest that centromeres assemble by self-loading of ParB DNA sliding clamps at parS. ParB CTPase is not related to known nucleotide hydrolases and might be a promising target for developing new classes of antibiotics.
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