RNA-BINDING DOMAIN OF THE A-PROTEIN COMPONENT OF THE U1 SMALL NUCLEAR RIBONUCLEOPROTEIN ANALYZED BY NMR-SPECTROSCOPY IS STRUCTURALLY SIMILAR TO RIBOSOMAL-PROTEINS
RNA-BINDING DOMAIN OF THE A-PROTEIN COMPONENT OF THE U1 SMALL NUCLEAR RIBONUCLEOPROTEIN ANALYZED BY NMR-SPECTROSCOPY IS STRUCTURALLY SIMILAR TO RIBOSOMAL-PROTEINS
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DOI：
10.1073/pnas.88.6.2495
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发表时间：
1991-03-01
影响因子：
11.1
通讯作者：
KEENE, JD
中科院分区：
文献类型：
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作者：
HOFFMAN, DW;QUERY, CC;KEENE, JD
RNA识别基序（RRM）几乎等于80个氨基酸组成的核心RNA结合结构域中发现的一个大家族的蛋白质参与RNA加工。通过使用NMR光谱分析了人U1小核核糖核蛋白（RNP）的A蛋白组分的U1 RNA结合结构域，其包含RRM序列。A蛋白的结构域是溶液中高度稳定的单体，由四条反向平行的β链和两条α螺旋组成。高度保守的RNP1和RNP2共有序列，含有先前建议参与核酸结合的残基，并置在相邻的β链中。对于RNA结合至关重要的保守芳族侧链聚集在分子表面上，邻近影响特定RNA序列识别的可变环。RRM的二级结构和拓扑结构与核糖体蛋白L12和L30相似，表明这两种类型的RNA相关蛋白之间存在遥远的进化关系。
An RNA recognition motif (RRM) of almost-equal-to 80 amino acids constitutes the core of RNA-binding domains found in a large family of proteins involved in RNA processing. The U1 RNA-binding domain of the A protein component of the human U1 small nuclear ribonucleoprotein (RNP), which encompasses the RRM sequence, was analyzed by using NMR spectroscopy. The domain of the A protein is a highly stable monomer in solution consisting of four antiparallel beta-strands and two alpha-helices. The highly conserved RNP1 and RNP2 consensus sequences, containing residues previously suggested to be involved in nucleic acid binding, are juxtaposed in adjacent beta-strands. Conserved aromatic side chains that are critical for RNA binding are clustered on the surface of the molecule adjacent to a variable loop that influences recognition of specific RNA sequences. The secondary structure and topology of the RRM are similar to those of ribosomal proteins L12 and L30, suggesting a distant evolutionary relationship between these two types of RNA-associated proteins.