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首页> 外文期刊>Journal of Cell Science >Specific and conserved sequences in D. melanogaster and C. elegans lamins and histone H2A mediate the attachment of lamins to chromosomes.
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Specific and conserved sequences in D. melanogaster and C. elegans lamins and histone H2A mediate the attachment of lamins to chromosomes.

机译：D. melanogaster和秀丽隐杆线虫lamins和组蛋白H2A中的特定和保守序列介导lamins与染色体的连接。

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摘要

The intimate association between nuclear lamins and chromatin is thought to regulate higher order chromatin organization. Previous studies have mapped a region between the rod domain and the Ig fold in the tail domain of Drosophila melanogaster lamin Dm0, which binds chromatin in vitro via the histone H2A/H2B dimer. This region contains an evolutionarily conserved nuclear localization signal (NLS) KRKR, and a sequence composed of the amino acids TRAT. Here we show that binding of lamin Dm0 to chromatin requires both NLS and TRAT sequences. Substituting either of the threonine residues in the TRAT sequence with negatively charged residues decreases the binding of lamin Dm0 to chromatin, indicating that this binding could be regulated by phosphorylation. Both lamin Dm0 and C. elegans Ce-lamin bind directly to histone H2A in vitro and this binding requires the NLS. The amino and carboxyl tail domains of histone H2A are each essential, but not sufficient, for binding to lamin Dm0; only a polypeptide containing both histone H2A tail domains binds efficiently to lamin Dm0. Taken together, these results suggest that specific residues in lamin Dm0 and histone H2A mediate the attachment of the nuclear lamina to chromosomes in vivo, which could have implications on the understanding of laminopathic diseases.
机译：核纤层蛋白和染色质之间的密切联系被认为调节了高级染色质的组织。先前的研究已经绘制了果蝇Lamin Dm0的杆结构域和尾结构域中Ig折叠之间的区域，该区域通过组蛋白H2A / H2B二聚体在体外结合染色质。该区域包含进化保守的核定位信号（NLS）KRKR，以及由氨基酸TRAT组成的序列。在这里，我们显示核纤层蛋白Dm0与染色质的结合需要NLS和TRAT序列。用带负电荷的残基取代TRAT序列中的任何一个苏氨酸残基会降低层粘连蛋白Dm0与染色质的结合，表明该结合可以通过磷酸化来调节。层粘连蛋白Dm0和秀丽隐杆线虫Ce-lamin在体外都直接与组蛋白H2A结合，这种结合需要NLS。组蛋白H2A的氨基和羧基尾结构域对于结合层粘连蛋白Dm0而言都是必不可少的，但不足以结合。只有包含两个组蛋白H2A尾部结构域的多肽才能有效结合层粘蛋白Dm0。综上所述，这些结果表明，lamin Dm0和组蛋白H2A中的特定残基在体内介导了核纤层对染色体的附着，这可能对理解lamopathic疾病有影响。

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