Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–13 of 13 results
Advanced filters: Author: Christian H. Haering Clear advanced filters

  • During mitosis, the two copies of each chromosome pair are held together by cohesin. Three subunits of cohesin form a ring structure and it has been proposed that the sister chromatids are tethered together by being encircled by cohesin rings. This paper provides the most direct evidence to date that cohesin rings topologically entrap two DNA molecules.

    • Christian H. Haering
    • Ana-Maria Farcas
    • Kim Nasmyth
    Research
    Nature
    Volume: 454, P: 297-301

  • Condensins organize chromosomes to allow proper segregation during mitosis or meiosis. Haering and colleagues show that the two HEAT-repeat subunits of the condensin complex, Ycg1 and Ycs4, bind DNA; this interaction stimulates ATPase activity of the SMC subunits and is required for condensin association with chromosomes.

    • Ilaria Piazza
    • Anna Rutkowska
    • Christian H Haering
    Research
    Nature Structural & Molecular Biology
    Volume: 21, P: 560-568

  • The condensin complex contributes to the compaction of eukaryotic chromosomes during mitosis and meiosis. How condensin organizes and compacts chromatin is now investigated by the introduction of specific cleavage sites into yeast condensin subunits. The results indicate that condensin forms a ring-like structure that encircles DNA.

    • Sara Cuylen
    • Jutta Metz
    • Christian H Haering
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 894-901

  • Cryo-EM structures of the S. cerevisiae condensin holo complex reveal that ATP binding triggers exchange of the two HEAT-repeat subunits bound to the SMC ATPase head domains, potentially leading to an interconversion of DNA-binding sites in the catalytic core of condensin that might form the basis of its DNA translocation and loop-extrusion activities.

    • Byung-Gil Lee
    • Fabian Merkel
    • Christian H. Haering
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 743-751

  • Single-molecule visualization shows that condensin—a motor protein that extrudes DNA in one direction only—can encounter and pass a second condensin molecule to form a new type of DNA loop that gathers DNA from both sides.

    • Eugene Kim
    • Jacob Kerssemakers
    • Cees Dekker
    Research
    Nature
    Volume: 579, P: 438-442

  • Atomic force microscopy imaging of yeast condensin indicates that condensin may extrude DNA by switching conformation between open O and collapsed B shapes, indicative of a type of scrunching model.

    • Je-Kyung Ryu
    • Allard J. Katan
    • Cees Dekker
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 1134-1141

  • Depletion of chromosome-associated cohesin leads to loss of topologically associating domains in interphase chromosomes, without affecting segregation into compartments, and instead, it unmasks a finer compartment structure that reflects local chromatin and transcriptional activity.

    • Wibke Schwarzer
    • Nezar Abdennur
    • Francois Spitz
    Research
    Nature
    Volume: 551, P: 51-56

  • Intertwining of DNA molecules frequently results in the formation of ‘ultrafine bridges’ between sister chromatids that need to be resolved during segregation of the chromatids into daughter cells. Although it has been established that these DNA bridges are coated by the helicase PICH, it has remained unknown how PICH assists in their resolution. A study now reveals that PICH directs the formation of positive DNA supercoiling in the presence of type I topoisomerases to promote the subsequent disentanglement of these DNA helices by type II topoisomerases. Remarkably, PICH might be able to reconfigure DNA topology by extruding loops of DNA while it moves along the double helix.

    • Shveta Bisht
    • Christian H. Haering
    News & Views
    Nature Structural & Molecular Biology
    Volume: 26, P: 252-253