A MAJOR NUCLEOLAR PROTEIN, NUCLEOLIN, INDUCES CHROMATIN DECONDENSATION BY BINDING TO HISTONE-H1
A MAJOR NUCLEOLAR PROTEIN, NUCLEOLIN, INDUCES CHROMATIN DECONDENSATION BY BINDING TO HISTONE-H1
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DOI：
10.1111/j.1432-1033.1988.tb14224.x
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发表时间：
1988-08-15
期刊：
影响因子：
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通讯作者：
AMALRIC, F
中科院分区：
文献类型：
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作者：
ERARD, MS;BELENGUER, P;AMALRIC, F
用圆二色谱探测染色质中DNA凝聚的程度，我们已经证明了一种主要的核仁蛋白，核仁素，可以解聚染色质。通过各种结合分析，我们表明核核素与组蛋白H1有很强的亲和力，并且磷酸化的N-末端结构域富含长链的酸性氨基酸，是这种离子相互作用的原因。其他实验清楚地表明，核素不能作为核小体核心组装或拆解因子，因此与核心组蛋白八聚体几乎没有亲和力。我们认为这种核仁蛋白通过与组蛋白H1结合来诱导染色质解缩，因此核仁可以被认为是一种高迁移率基团类型的蛋白质。
Using circular dichroism to probe the extent of DNA condensation in chromatin, we have demonstrated that a major nucleolar protein, nucleolin, can decondense chromatin. By means of various binding assays we show that neucleolin has a strong affinity for histone H1 and that the phosphorylated N-terminal domain, rich in lengthy stretches of acidic amino acids, is responsible for this ionic interaction. Additional experiments clearly demonstrate that nucleolin is unable to act as a nucleosome core assembly or disassembly factor and hence has little affinity for the core histone octamer. We propose that this nucleolar protein induces chromatin decondensation by binding to histone H1, and that nucleolin can therefore be regarded as a protein of the high-mobility-group type.