CENH3 interacts with the centromeric retrotransposon cereba and GC-rich satellites and locates to centromeric substructures in barley

CENH3 interacts with the centromeric retrotransposon cereba and GC-rich satellites and locates to centromeric substructures in barley
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DOI:
10.1007/s00412-007-0102-z
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发表时间:
2007-06-01
期刊:
影响因子:
1.6
通讯作者:
Endo, Takashi R.
Endo, Takashi R.
中科院分区:
生物学3区
文献类型:
--
作者:
Houben, Andreas;Schroeder-Reiter, Elizabeth;Endo, Takashi R.

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着丝粒特异性组蛋白H3(CENH3)的染色体定位是活性着丝粒的动粒复合物的组装位点。染色质免疫沉淀数据表明,CENH 3相互作用,在大麦与cereba,一个着丝粒逆转录元件(CR)的元件之间保守的谷物着丝粒和大麦特定的GC丰富的着丝粒卫星序列。抗CENH3信号在延长的染色质纤维总是共定位与着丝粒序列,但不包括整个区域所覆盖的这样的着丝粒重复。这表明CENH3蛋白仅与一部分着丝粒重复序列结合。在有丝分裂中期,CENH3,组蛋白H3,和丝氨酸10磷酸化组蛋白H3占主导地位的着丝粒的不同结构的亚结构域内,所示的免疫金标记的高分辨率扫描电子显微镜。
The chromosomal location of centromere-specific histone H3 (CENH3) is the assembly site for the kinetochore complex of active centromeres. Chromatin immunoprecipitation data indicated that CENH3 interacts in barley with cereba, a centromeric retroelement (CR)-like element conserved among cereal centromeres and barley-specific GC-rich centromeric satellite sequences. Anti-CENH3 signals on extended chromatin fibers always colocalized with the centromeric sequences but did not encompass the entire area covered by such centromeric repeats. This indicates that the CENH3 protein is bound only to a fraction of the centromeric repeats. At mitotic metaphase, CENH3, histone H3, and serine 10 phosphorylated histone H3 predominated within distinct structural subdomains of the centromere, as demonstrated by immunogold labeling for high resolution scanning electron microscopy.