首页> 美国卫生研究院文献>The EMBO Journal >The hbrm and BRG-1 proteins components of the human SNF/SWI complex are phosphorylated and excluded from the condensed chromosomes during mitosis.
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The hbrm and BRG-1 proteins components of the human SNF/SWI complex are phosphorylated and excluded from the condensed chromosomes during mitosis.

机译:hbrm和BRG-1蛋白是人SNF / SWI复合体的组成部分在有丝分裂过程中被磷酸化并从浓缩染色体中排除。

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摘要

In yeast, the SNF/SWI complex is believed to regulate transcription by locally altering the chromatin structure. At the present time, three human homologues of yeast SNF/SWI proteins have been characterized: hbrm and BRG-1, homologues of SNF2/SWI2, and hSNF5, a homologue of SNF5. We show here that, during mitosis, hbrm and BRG-1 are phosphorylated and excluded from the condensed chromosomes. In this phase of the cell cycle, the level of hbrm protein is also strongly reduced, whereas the level of BRG-1 remains constant. The mitotic phosphorylation of hbrm and BRG-1 is found not to disrupt the association of these proteins with hSNF5 but correlates with a decreased affinity for the nuclear structure in early M phase. We suggest that chromosomal exclusion of the human SNF/SWI complex at the G2-M transition could be part of the mechanism leading to transcriptional arrest during mitosis.
机译:在酵母中,据信SNF / SWI复合物通过局部改变染色质结构来调节转录。目前,已经表征了酵母SNF / SWI蛋白的三种人类同源物:hbrm和BRG-1,SNF2 / SWI2的同源物,和hSNF5,SNF5的同源物。我们在这里显示,在有丝分裂期间,hbrm和BRG-1被磷酸化并从浓缩染色体中排除。在细胞周期的这一阶段,hbrm蛋白的水平也大大降低,而BRG-1的水平保持恒定。发现hbrm和BRG-1的有丝分裂磷酸化不会破坏这些蛋白与hSNF5的结合,但与早期M期对核结构的亲和力降低相关。我们建议在G2-M过渡期人类SNF / SWI复合体的染色体排斥可能是导致有丝分裂期间转录停滞的机制的一部分。

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