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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Identification of the single-strand telomeric DNA binding domain of the Saccharomyces cerevisiae Cdc13 protein
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Identification of the single-strand telomeric DNA binding domain of the Saccharomyces cerevisiae Cdc13 protein

机译：酿酒酵母Cdc13蛋白的单链端粒DNA结合域的鉴定。

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摘要

The CDC13 gene of Saccharomyces cerevisiae is required both to protect telomeric DNA and to ensure proper function of yeast telomerase in vivo. We have previously demonstrated that Cdc13p has a high affinity single-strand telomeric DNA binding activity. although the primary amino acid sequence of Cdc13p has no previously characterized DNA binding motifs. We report here mapping of the Cdc13 DNA binding domain by a combina- tion of proteolysis mapping and deletion cloning. The DNA binding domain maps to residues S57--694 of the 924-amino acid Cdc13 polypeptide, within the most basic region of Cdc13p. A slightly larger version of this domain can be efficiently ex- pressed in EScherichia coli as a soluble small protein, with DNA binding properties comparable to those of the full-length pro- tein. A single amino acid missense mutation within this domain results in thermolabile DNA binding and conditional lethality in yeast, consistent with the prediction that DNA binding should be essential for CDC13 function. These results show that Cdc13p contains a discrete substructure responsible for DNA binding and should facilitate structural characterization of this telomere binding protein.
机译：酿酒酵母的CDC13基因既需要保护端粒DNA，又要确保酵母端粒酶在体内的正常功能。我们以前已经证明了Cdc13p具有高亲和力的单链端粒DNA结合活性。尽管Cdc13p的主要氨基酸序列没有以前鉴定过的DNA结合基序。我们在此报告通过蛋白水解图谱和缺失克隆的结合来绘制Cdc13 DNA结合域的图谱。 DNA结合结构域映射到Cdc13p最基本区域内的924个氨基酸的Cdc13多肽的S57--694残基。该结构域的稍大版本可以作为可溶性小蛋白在大肠杆菌中高效表达，其DNA结合特性可与全长蛋白相媲美。该结构域内的单个氨基酸错义突变会导致不耐热的DNA结合和酵母中的条件杀伤力，这与DNA结合对于CDC13功能必不可少的预测相一致。这些结果表明，Cdc13p包含负责DNA结合的离散亚结构，应有助于端粒结合蛋白的结构表征。

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