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首页> 外文期刊>Biochemistry >Chromatin Condensing Functions of the Linker Histone C-Terminal Domain Are Mediated by Specific Amino Acid Composition and Intrinsic Protein Disorder
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Chromatin Condensing Functions of the Linker Histone C-Terminal Domain Are Mediated by Specific Amino Acid Composition and Intrinsic Protein Disorder

机译：接头组蛋白C末端结构域的染色质浓缩功能由特定氨基酸组成和内在蛋白紊乱介导。

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摘要

Linker histones bind to the nucleosomes and linker DNA of chromatin fibers, causing changes in linker DNA structure and stabilization of higher order folded and oligomeric chromatin structures. Linker histones affect chromatin structure acting primarily through their 100-residue C-terminal domain (CTD). We have previously shown that the ability of the linker histone H1° to alter chromatin structure was localized to two discontinuous 24-/25-residue CTD regions (Lu, X., and Hansen, J. C. (2004) J. Biol. Chem. 279, 8701−8707). To determine the biochemical basis for these results, we have characterized chromatin model systems assembled with endogenous mouse somatic H1 isoforms or recombinant H1° CTD mutants in which the primary sequence has been scrambled, the amino acid composition mutated, or the location of various CTD regions swapped. Our results indicate that specific amino acid composition plays a fundamental role in molecular recognition and function by the H1 CTD. Additionally, these experiments support a new molecular model for CTD function and provide a biochemical basis for the redundancy observed in H1 isoform knockout experiments in vivo.
机译：接头组蛋白与染色质纤维的核小体和接头DNA结合，导致接头DNA结构发生变化，并使高阶折叠和寡聚染色质结构稳定。接头组蛋白主要通过其100个残基的C末端结构域（CTD）影响染色质结构。先前我们已经表明，接头组蛋白H1°改变染色质结构的能力被定位于两个不连续的24/25残基CTD区域（Lu，X。和Hansen，JC（2004）J.Biol.Chem.279。 ，8701-8707）。为了确定这些结果的生物化学基础，我们表征了与内源性小鼠体细胞H1亚型或重组H1°CTD突变体组装而成的染色质模型系统，其中原始序列已被打乱，氨基酸组成发生突变或各个CTD区域的位置交换。我们的结果表明，特定的氨基酸组成在H1 CTD的分子识别和功能中起着基本作用。此外，这些实验支持CTD功能的新分子模型，并为体内H1亚型敲除实验中观察到的冗余提供了生化基础。

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    《Biochemistry》 |2009年第1期|p.164-172|共9页
  • 作者

    Xu Lu Barbara Hamkalo Missag H. Parseghian and Jeffrey C. Hansen;

  • 作者单位

    Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870, Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, California 92697, and Department of Research and Development, Peregrine Pharmaceuticals, 14272 Franklin Avenue, Tustin, California 92780;

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