Chromosome organization by a conserved condensin-ParB system in the actinobacterium Corynebacterium glutamicum

Kati Böhm, Giacomo Giacomelli, Andreas Schmidt, Axel Imhof, Romain Koszul, Martial Marbouty () and Marc Bramkamp ()
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Kati Böhm: Ludwig-Maximilians-Universität München, Fakultät Biologie
Giacomo Giacomelli: Ludwig-Maximilians-Universität München, Fakultät Biologie
Andreas Schmidt: Biomedical Center, Protein Analysis Unit, Faculty of Medicine, Ludwig-Maximilians-Universität München
Axel Imhof: Biomedical Center, Protein Analysis Unit, Faculty of Medicine, Ludwig-Maximilians-Universität München
Romain Koszul: Institut Pasteur, Unité Régulation Spatiales des Génomes, UMR3525, CNRS
Martial Marbouty: Institut Pasteur, Unité Régulation Spatiales des Génomes, UMR3525, CNRS
Marc Bramkamp: Ludwig-Maximilians-Universität München, Fakultät Biologie

Nature Communications, 2020, vol. 11, issue 1, 1-17

Abstract: Abstract Higher-order chromosome folding and segregation are tightly regulated in all domains of life. In bacteria, details on nucleoid organization regulatory mechanisms and function remain poorly characterized, especially in non-model species. Here, we investigate the role of DNA-partitioning protein ParB and SMC condensin complexes in the actinobacterium Corynebacterium glutamicum. Chromosome conformation capture reveals SMC-mediated long-range interactions around ten centromere-like parS sites clustered at the replication origin (oriC). At least one oriC-proximal parS site is necessary for reliable chromosome segregation. We use chromatin immunoprecipitation and photoactivated single-molecule localization microscopy to show the formation of distinct, parS-dependent ParB-nucleoprotein subclusters. We further show that SMC/ScpAB complexes, loaded via ParB at parS sites, mediate chromosomal inter-arm contacts (as previously shown in Bacillus subtilis). However, the MukBEF-like SMC complex MksBEFG does not contribute to chromosomal DNA-folding; instead, this complex is involved in plasmid maintenance and interacts with the polar oriC-tethering factor DivIVA. Our results complement current models of ParB-SMC/ScpAB crosstalk and show that some condensin complexes evolved functions that are apparently uncoupled from chromosome folding.

Date: 2020
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DOI: 10.1038/s41467-020-15238-4

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