Query C C, Bentley R C, Keene J D
Department of Microbiology and Immunology, Duke University Medical Center, Durham, North Carolina 27710.
Mol Cell Biol. 1989 Nov;9(11):4872-81. doi: 10.1128/mcb.9.11.4872-4881.1989.
We have defined the nucleotide sequence of a protein-binding domain within U1 RNA that specifically recognizes and binds both to a U1 small nuclear ribonucleoprotein component (the 70K protein) and to the previously defined RNA-binding domain of the 70K protein. We have investigated direct interactions between purified U1 RNA and 70K protein by reconstitution in vitro. Thirty-one nucleotides of U1 RNA, corresponding to stem-loop I, were required for this interaction. Nucleotides at the 5' end of U1 RNA that are involved in base pairing with the 5' splice site of pre-mRNA were not required for binding. In contrast to other reports, these findings demonstrate that a specific domain of U1 RNA can bind directly to the 70K protein independently of any other snRNP-associated proteins.
我们已经确定了U1 RNA中一个蛋白质结合结构域的核苷酸序列,该结构域能特异性识别并结合U1小核核糖核蛋白组分(70K蛋白)以及70K蛋白先前定义的RNA结合结构域。我们通过体外重组研究了纯化的U1 RNA与70K蛋白之间的直接相互作用。这种相互作用需要U1 RNA中对应于茎环I的31个核苷酸。U1 RNA 5'端与前体mRNA 5'剪接位点进行碱基配对的核苷酸对于结合并非必需。与其他报道相反,这些发现表明U1 RNA的一个特定结构域可以独立于任何其他与小核核糖核蛋白相关的蛋白质直接结合70K蛋白。