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The Est1 Subunit of Yeast Telomerase Binds the Tlc1 Telomerase RNA

机译:酵母端粒酶的Est1亚基与Tlc1端粒酶RNA结合

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Est1 is a component of yeast telomerase, and est1mutants have senescence and telomere loss phenotypes. The exact function of Est1 is not known, and it is not homologous to components of other telomerases. We previously showed that Est1 protein coimmunoprecipitates with Tlc1 (the telomerase RNA) as well as with telomerase activity. Est1 has homology to Ebs1, an uncharacterized yeast open reading frame product, including homology to a putative RNA recognition motif (RRM) of Ebs1. Deletion of EBS1 results in short telomeres. We created point mutations in a putative RRM of Est1. One mutant was unable to complement either the senescence or the telomere loss phenotype of est1 mutants. Furthermore, the mutant protein no longer coprecipitated with the Tlc1 telomerase RNA. Mutants defective in the binding of Tlc1 RNA were nevertheless capable of binding single-stranded TG-rich DNA. Our data suggest that an important role of Est1 in the telomerase complex is to bind to the Tlc1 telomerase RNA via an RRM. Since Est1 can also bind telomeric DNA, Est1 may tether telomerase to the telomere.
机译:Est1是酵母端粒酶的组成部分,而 est1 突变体具有衰老和端粒丢失表型。 Est1的确切功能尚不清楚,并且与其他端粒酶的成分不同源。我们先前显示,Est1蛋白与Tlc1(端粒酶RNA)以及端粒酶活性共免疫沉淀。 Est1与Ebs1(未鉴定的酵母开放阅读框架产品)具有同源性,包括与Ebs1的假定RNA识别基序(RRM)同源。删除 EBS1 会导致端粒变短。我们在Est1的假定RRM中创建了点突变。一个突变体不能补充 est1 突变体的衰老或端粒丢失表型。此外,突变蛋白不再与Tlc1端粒酶RNA共沉淀。 Tlc1 RNA结合缺陷的突变体仍然能够结合富含TG的单链DNA。我们的数据表明,Est1在端粒酶复合物中的重要作用是通过RRM与Tlc1端粒酶RNA结合。由于Est1也可以结合端粒DNA,因此Est1可以将端粒酶拴在端粒上。

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