Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation

Josh P. Prince, Jani R. Bolla, Gemma L. M. Fisher, Jarno Mäkelä, Marjorie Fournier, Carol V. Robinson, Lidia K. Arciszewska and David J. Sherratt ()
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Josh P. Prince: University of Oxford
Jani R. Bolla: Physical and Theoretical Chemistry Laboratory, University of Oxford
Gemma L. M. Fisher: University of Oxford
Jarno Mäkelä: University of Oxford
Marjorie Fournier: University of Oxford
Carol V. Robinson: Physical and Theoretical Chemistry Laboratory, University of Oxford
Lidia K. Arciszewska: University of Oxford
David J. Sherratt: University of Oxford

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract Structural Maintenance of Chromosomes (SMC) complexes act ubiquitously to compact DNA linearly, thereby facilitating 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. Dimeric SMC proteins interact with essential accessory proteins, kleisins that bridge the two subunits of an SMC dimer, and HAWK/KITE proteins that interact with kleisins. The ATPase activity of the Escherichia coli SMC protein, MukB, which is essential for its in vivo function, requires its interaction with the dimeric kleisin, MukF that in turn interacts with the KITE protein, MukE. Here we demonstrate that, in addition, MukB interacts specifically with Acyl Carrier Protein (AcpP) that has essential functions in fatty acid synthesis. We characterize the AcpP interaction at the joint of the MukB coiled-coil and show that the interaction is necessary for MukB ATPase and for MukBEF function in vivo.

Date: 2021
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DOI: 10.1038/s41467-021-27107-9

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