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Condensin association with chromosomes depends on a DNA binding domain formed by its HEAT-repeat subunits


ABSTRACT: Condensin protein complexes play central roles in the three-dimensional organization of chromosomes during mitotic and meiotic cell divisions. How condensin interacts with its chromatin substrates to promote sister chromatid decatenation and segregation is largely unknown. Previous work suggested that condensin, in addition to encircling chromatin fibers topologically within the large ring-shaped structure formed by its structural maintenance of chromosomes (SMC) and kleisin subunits, contacts DNA directly. Here we describe the discovery of a binding domain for double-stranded DNA helices formed by condensinM-bM-^@M-^Ys HEAT-repeat subunits. Using detailed mapping data of the interfaces between the HEAT-repeat and the kleisin subunits, we generated mutant complexes that lack the Ycg1/CAP-G HEAT-repeat subunit. These tetrameric condensin complexes fail to associate stably with chromosomes in yeast and human cells. We suggest that condensin controls chromosome architecture by stabilizing chromatin loops of chromatin fibers through interaction with its unconventional HEAT-repeat DNA binding domain. Analysis of condensin binding genomewide in a wild type and a condensin mutant

ORGANISM(S): Saccharomyces cerevisiae

SUBMITTER: Ilaria Piazza 

PROVIDER: E-GEOD-55948 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Association of condensin with chromosomes depends on DNA binding by its HEAT-repeat subunits.

Piazza Ilaria I   Rutkowska Anna A   Ori Alessandro A   Walczak Marta M   Metz Jutta J   Pelechano Vicent V   Beck Martin M   Haering Christian H CH  

Nature structural & molecular biology 20140518 6


Condensin complexes have central roles in the three-dimensional organization of chromosomes during cell divisions, but how they interact with chromatin to promote chromosome segregation is largely unknown. Previous work has suggested that condensin, in addition to encircling chromatin fibers topologically within the ring-shaped structure formed by its SMC and kleisin subunits, contacts DNA directly. Here we describe the discovery of a binding domain for double-stranded DNA formed by the two HEAT  ...[more]

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