SMC condensin entraps chromosomal DNA by an ATP hydrolysis dependent loading mechanism in Bacillus subtilis

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Smc-ScpAB forms elongated, annular structures that promote chromosome segregation, presumably by compacting and resolving sister DNA molecules. The mechanistic basis for its action, however, is only poorly understood. Here, we have established a physical assay to determine whether the binding of condensin to native chromosomes in Bacillus subtilis involves entrapment of DNA by the Smc-ScpAB ring. To do so, we have chemically cross-linked the three ring interfaces in Smc-ScpAB and thereafter isolated intact chromosomes under protein denaturing conditions. Exclusively species of Smc-ScpA, which were previously cross-linked into covalent rings, remained associated with chromosomal DNA. DNA entrapment is abolished by mutations that interfere with the Smc ATPase cycle and strongly reduced when the recruitment factor ParB is deleted, implying that most Smc-ScpAB is loaded onto the chromosome at parS sites near the replication origin. We furthermore report a physical interaction between native Smc-ScpAB and chromosomal DNA fragments.
Publisher
ELIFE SCIENCES PUBLICATIONS LTD
Issue Date
2015-05
Language
English
Article Type
Article
Keywords

PROTEIN SPO0J; B. SUBTILIS; IN-VITRO; COHESIN; COMPLEX; SEGREGATION; PARB; REPLICATION; CELLS; LOCALIZATION

Citation

ELIFE, v.4

ISSN
2050-084X
DOI
10.7554/eLife.06659
URI
http://hdl.handle.net/10203/209075
Appears in Collection
BS-Journal Papers(저널논문)
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