bioRxiv preprint doi: https://doi.org/10.1101/2021.04.12.439405; this version posted April 12, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. ARTICLE Acyl Carrier Protein is essential for MukBEF action in Escherichia coli chromosome organization-segregation Josh P. Prince1, Jani R. Bolla2, 3, Gemma L. M. Fisher1, Jarno Mäkelä1, Carol V. Robinson2, 3, Lidia K. Arciszewska1 and David J. Sherratt1* 1 Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK 2 Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, UK 3 The Kavli Institute for Nanoscience Discovery, South Parks Road, Oxford OX1 3QU, UK * To whom correspondence should be addressed. Tel: +44 1865 613237; Fax: +44 1865 613213; Email:
[email protected] Present Address: Josh P. Prince: Meiosis Group, Medical Research Council London Institute of Medical Science, Du Cane Road, London W12 0NN, UK, Gemma L.M. Fisher, Cell Cycle Group, Medical Research Council London Institute of Medical Science, Du Cane Road, London W12 0NN, UK and Jarno Mäkelä, ChEM-H Institute, Stanford University, 290 Jane Stanford Way, CA 94305, US Keywords Acyl Carrier Protein/SMC/ MukBEF/ Escherichia coli/ chromosome organization Abstract Structural Maintenance of Chromosomes (SMC) complexes contribute ubiquitously to chromosome organization-segregation. SMC proteins have a conserved architecture, with a dimerization hinge and an ATPase head domain separated by a long antiparallel intramolecular coiled-coil.