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  • American Association for the Advancement of Science (AAAS)  (3)
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  • American Association for the Advancement of Science (AAAS)  (3)
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  • 1
    Online Resource
    Online Resource
    American Association for the Advancement of Science (AAAS) ; 2001
    In:  Science Vol. 294, No. 5551 ( 2001-12-21), p. 2539-2542
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 294, No. 5551 ( 2001-12-21), p. 2539-2542
    Abstract: Centromeres are heterochromatic in many organisms, but the mitotic function of this silent chromatin remains unknown. During cell division, newly replicated sister chromatids must cohere until anaphase when Scc1/Rad21–mediated cohesion is destroyed. In metazoans, chromosome arm cohesins dissociate during prophase, leaving centromeres as the only linkage before anaphase. It is not known what distinguishes centromere cohesion from arm cohesion. Fission yeast Swi6 (a Heterochromatin protein 1 counterpart) is a component of silent heterochromatin. Here we show that this heterochromatin is specifically required for cohesion between sister centromeres. Swi6 is required for association of Rad21-cohesin with centromeres but not along chromosome arms and, thus, acts to distinguish centromere from arm cohesion. Therefore, one function of centromeric heterochromatin is to attract cohesin, thereby ensuring sister centromere cohesion and proper chromosome segregation.
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    RVK:
    RVK:
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2001
    detail.hit.zdb_id: 128410-1
    detail.hit.zdb_id: 2066996-3
    detail.hit.zdb_id: 2060783-0
    SSG: 11
    Location Call Number Limitation Availability
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  • 2
    Online Resource
    Online Resource
    American Association for the Advancement of Science (AAAS) ; 2010
    In:  Science Vol. 327, No. 5962 ( 2010-01-08), p. 150-151
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 327, No. 5962 ( 2010-01-08), p. 150-151
    Abstract: Accurate chromosome segregation during eukaryotic cell division requires the timely release of cohesion between duplicated chromosomes so that they may separate into two daughter cells. Errors in this process have been linked to cancer progression, infertility, and debilitating genetic diseases such as Down syndrome. A surveillance mechanism known as the spindle assembly checkpoint delays this release until all chromosome pairs are properly attached to a structure called the mitotic spindle. The enzyme Bub1 is essential for this checkpoint, but the targets of its phosphorylation activity have been elusive. On page 172 of this issue, Kawashima et al. ( 1 ) report that histone H2A—a protein associated with DNA within chromosomes—is a substrate of Bub1, and that H2A phosphorylation directs subsequent events that control chromatid cohesion and the checkpoint mechanism during the early stages of cell division.
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    RVK:
    RVK:
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 2010
    detail.hit.zdb_id: 128410-1
    detail.hit.zdb_id: 2066996-3
    detail.hit.zdb_id: 2060783-0
    SSG: 11
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 3
    Online Resource
    Online Resource
    American Association for the Advancement of Science (AAAS) ; 1995
    In:  Science Vol. 269, No. 5229 ( 1995-09-08), p. 1429-1431
    In: Science, American Association for the Advancement of Science (AAAS), Vol. 269, No. 5229 ( 1995-09-08), p. 1429-1431
    Type of Medium: Online Resource
    ISSN: 0036-8075 , 1095-9203
    RVK:
    RVK:
    Language: English
    Publisher: American Association for the Advancement of Science (AAAS)
    Publication Date: 1995
    detail.hit.zdb_id: 128410-1
    detail.hit.zdb_id: 2066996-3
    detail.hit.zdb_id: 2060783-0
    SSG: 11
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
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