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Cell cycle-dependent deposition of CENP-A requires the Dos1/2-Cdc20 complex.(GENETICS)(Author abstract)

Gonzalez, Marlyn ; He, Haijin ; Sun, Siyu ; Li, Chen ; Li, Fei

Proceedings of the National Academy of Sciences of the United States, Jan 8, 2013, Vol.110(2), p.606(6) [Tạp chí có phản biện]

ISSN: 0027-8424

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  • Nhan đề:
    Cell cycle-dependent deposition of CENP-A requires the Dos1/2-Cdc20 complex.(GENETICS)(Author abstract)
  • Tác giả: Gonzalez, Marlyn ; He, Haijin ; Sun, Siyu ; Li, Chen ; Li, Fei
  • Chủ đề: Dna Replication -- Research ; Cell Cycle -- Research ; Methylation -- Research ; Rna -- Research
  • Là 1 phần của: Proceedings of the National Academy of Sciences of the United States, Jan 8, 2013, Vol.110(2), p.606(6)
  • Mô tả: Centromeric histone CENP-A, a variant of canonical histone H3, plays a central role in proper chromosome segregation. Loading of CENP-A at centromeres is cell cycle-regulated: parental CENP-A is deposited at centromeres during S phase, whereas newly synthesized CENP-A is deposited during later stages of the cell cycle. The mechanisms involved in deposition of CENP-A at centromeres during S phase remain poorly understood. In fission yeast, loading of CENP-A during S phase is regulated by the GATA-type factor, Ams2. Here we show that the Dos1/2-Cdc20 complex, previously characterized as a silencing complex essential for inheritance of H3K9 methylation during S phase, is also required for localization of CENP-[A.sup.cnp1] at centromeres at this stage. Disruption of Dos1 (also known as Raf1/CIr8/Cmc1), Dos2 (also known as Raf2/CIr7/Cmc2), or Cdc20, a DNA polymerase epsilon subunit, results in dissociation of CENP-A from centromeres and mislocalization of the protein to noncentromeric sites. All three mutants display spindle disorganization and mitotic defects. Inactivation of Dos1 or Cdc20 also results in accumulation of non-coding RNA transcripts from centromeric cores, a feature common to mutants affecting kinetochore integrity. We further find that Dos1 physically associates with Ams2 and is required for the association of Ams2 with centromeric cores during S phase. Finally, we show that Dos2 associates with centromeric cores during S phase and that its recruitment to centromeric cores depends on Cdc20. This study identifies a physical link between DNA replication and CENP-A assembly machinery and provides mechanistic insight into how CENP-A is faithfully inherited during S phase. epigenetics | heterochromatin doi/10.1073/pnas.1214874110
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0027-8424

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