Journal
NATURE COMMUNICATIONS
Volume 11, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-020-15238-4
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Funding
- Deutsche Forschungsgemeinschaft [326464754, TRR174, BR2815/6-2]
- Ministry of Science and Education [BMBF: 031A302 e:Bio-Modul II: 0.6 plus]
- European Research Council under the Horizon 2020 Program (ERC) [260822]
- Agence Nationale pour la Recherche [HiResBac ANR-15-CE11-0023-03]
- JPI-EC-AMR STARCS [ANR-16-JPEC-0003-05]
- Agence Nationale de la Recherche (ANR) [ANR-16-JPEC-0003] Funding Source: Agence Nationale de la Recherche (ANR)
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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.
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