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.

E. coli MukBEF is an SMC complex that plays key roles in chromosome organization-segregation. Here the authors show that the interaction between MukBEF and the Acyl Carrier Protein (AcpP) is essential for MukBEF activity in vitro (ATPase) and in vivo.

Details

Title
Acyl carrier protein promotes MukBEF action in Escherichia coli chromosome organization-segregation
Author
Prince, Josh P 1   VIAFID ORCID Logo  ; Bolla, Jani R 2   VIAFID ORCID Logo  ; Fisher Gemma L M 3   VIAFID ORCID Logo  ; Mäkelä Jarno 4   VIAFID ORCID Logo  ; Fournier, Marjorie 5 ; Robinson, Carol V 6   VIAFID ORCID Logo  ; Arciszewska, Lidia K 5 ; Sherratt, David J 5   VIAFID ORCID Logo 

1  University of Oxford, Department of Biochemistry, Oxford, UK (GRID:grid.4991.5) (ISNI:0000 0004 1936 8948); Meiosis Group, Medical Research Council London Institute of Medical Sciences, London, UK (GRID:grid.14105.31) (ISNI:0000000122478951) 
2  Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK (GRID:grid.4991.5) (ISNI:0000 0004 1936 8948); The Kavli Institute for Nanoscience Discovery, Oxford, UK (GRID:grid.4991.5); University of Oxford, Department of Plant Sciences, Oxford, UK (GRID:grid.4991.5) (ISNI:0000 0004 1936 8948) 
3  University of Oxford, Department of Biochemistry, Oxford, UK (GRID:grid.4991.5) (ISNI:0000 0004 1936 8948); DNA Motors Group, Medical Research Council London Institute of Medical Sciences, London, UK (GRID:grid.14105.31) (ISNI:0000000122478951) 
4  University of Oxford, Department of Biochemistry, Oxford, UK (GRID:grid.4991.5) (ISNI:0000 0004 1936 8948); ChEM-H Institute, Stanford University, Stanford, USA (GRID:grid.168010.e) (ISNI:0000000419368956) 
5  University of Oxford, Department of Biochemistry, Oxford, UK (GRID:grid.4991.5) (ISNI:0000 0004 1936 8948) 
6  Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford, UK (GRID:grid.4991.5) (ISNI:0000 0004 1936 8948); The Kavli Institute for Nanoscience Discovery, Oxford, UK (GRID:grid.4991.5) 
Publication year
2021
Publication date
2021
Publisher
Nature Publishing Group
e-ISSN
20411723
Source type
Scholarly Journal
Language of publication
English
DOI
https://doi.org/10.1038/s41467-021-27107-9
ProQuest document ID
2598833822
Copyright
© The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.