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

Autor: Prince JP; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.; Meiosis Group, Medical Research Council London Institute of Medical Sciences, Du Cane Road, London, W12 0NN, UK., Bolla JR; Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.; The Kavli Institute for Nanoscience Discovery, South Parks Road, Oxford, OX1 3QU, UK.; Department of Plant Sciences, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK., Fisher GLM; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.; DNA Motors Group, Medical Research Council London Institute of Medical Sciences, Du Cane Road, London, W12 0NN, UK., Mäkelä J; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.; ChEM-H Institute, Stanford University, 290 Jane Stanford Way, Stanford, CA, 94305, USA., Fournier M; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK., Robinson CV; Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK.; The Kavli Institute for Nanoscience Discovery, South Parks Road, Oxford, OX1 3QU, UK., Arciszewska LK; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK., Sherratt DJ; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. david.sherratt@bioch.ox.ac.uk.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2021 Nov 18; Vol. 12 (1), pp. 6721. Date of Electronic Publication: 2021 Nov 18.
DOI: 10.1038/s41467-021-27107-9
Abstrakt: 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.
(© 2021. The Author(s).)
Databáze: MEDLINE
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