Telomere DNA recognition in Saccharomycotina yeast: potential lessons for the co-evolution of ssDNA and dsDNA-binding proteins and their target sites.

Telomere DNA recognition in Saccharomycotina yeast: potential lessons for the co-evolution of ssDNA and dsDNA-binding proteins and their target sites.
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DOI:
10.3389/fgene.2015.00162
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发表时间:
2015
影响因子:
3.7
通讯作者:
Lue NF
Lue NF
中科院分区:
生物学3区
文献类型:
--
作者:
Steinberg-Neifach O;Lue NF

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原则上,端粒重复序列的改变预计会破坏赋予染色体末端稳定性的保护性核蛋白复合物,因此在进化中相对罕见。事实上,不同门的许多生物都有一个典型的6 bp的端粒重复单元(5 ' -TTAGGG-3 ' /5 ' -CCCTAA-3 '),这表明它们都来自一个携带这种重复序列的祖先。更值得注意的是,在出芽酵母的酵母菌亚门中,分布着极其不同的端粒序列。这些序列与典型端粒重复序列的区别在于它们较长,偶尔退化,并且通常不富含g / c。尽管端粒重复序列不同,但迄今为止的研究表明,在Saccharomycotina酵母中,单链和双链端粒结合蛋白家族(即Cdc13和Rap1家族)负责端粒保护。因此,蛋白质家族成员的识别机制为理解dna结合蛋白和同源靶序列的共同进化提供了信息范式。现有数据表明,DNA识别问题有三种潜在的、相互关联的解决方案:(i)识别蛋白的复制和功能修饰;(ii)组合识别目标位点;(iii) dna结合蛋白的识别表面的灵活性,以采用不同的构象。证据支持这些解决方案和相关性的这些解决方案,以其他dna -蛋白质调控系统进行了讨论。
In principle, alterations in the telomere repeat sequence would be expected to disrupt the protective nucleoprotein complexes that confer stability to chromosome ends, and hence relatively rare events in evolution. Indeed, numerous organisms in diverse phyla share a canonical 6 bp telomere repeat unit (5′-TTAGGG-3′/5′-CCCTAA-3′), suggesting common descent from an ancestor that carries this particular repeat. All the more remarkable, then, are the extraordinarily divergent telomere sequences that populate the Saccharomycotina subphylum of budding yeast. These sequences are distinguished from the canonical telomere repeat in being long, occasionally degenerate, and frequently non-G/C-rich. Despite the divergent telomere repeat sequences, studies to date indicate that the same families of single-strand and double-strand telomere binding proteins (i.e., the Cdc13 and Rap1 families) are responsible for telomere protection in Saccharomycotina yeast. The recognition mechanisms of the protein family members therefore offer an informative paradigm for understanding the co-evolution of DNA-binding proteins and the cognate target sequences. Existing data suggest three potential, inter-related solutions to the DNA recognition problem: (i) duplication of the recognition protein and functional modification; (ii) combinatorial recognition of target site; and (iii) flexibility of the recognition surfaces of the DNA-binding proteins to adopt alternative conformations. Evidence in support of these solutions and the relevance of these solutions to other DNA-protein regulatory systems are discussed.
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