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首页> 外文期刊>Journal of Molecular Biology >HNRNP A1 SELECTIVELY INTERACTS THROUGH ITS GLY-RICH DOMAIN WITH DIFFERENT RNA-BINDING PROTEINS
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HNRNP A1 SELECTIVELY INTERACTS THROUGH ITS GLY-RICH DOMAIN WITH DIFFERENT RNA-BINDING PROTEINS

机译：HNRNP A1通过其富含糖的域与不同的RNA结合蛋白选择性地相互作用

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摘要

Heterogeneous nuclear ribonucleoproteins (hnRNPs) are abundant nuclear polypeptides, most likely involved in different steps of pre-mRNA processing. Protein A1 (34 kDa), a prominent member of the hnRNP family, seems to act by modulating the RNA secondary structure and by antagonizing some splicing factors (SR proteins) in splice-site selection and exon skipping/inclusion. A role of A1 in the nucleo-cytoplasmic transport of RNA has also been proposed. These activities might depend not only on the RNA-binding properties of the protein but also on specific protein-protein interactions. Here we report that A1 can indeed selectively interact, in vitro, both with itself and. with other hnRNP basic ''core'' proteins. Such selective binding is mediated exclusively by the Gly-rich C-terminal domain, where a novel protein-binding motif constituted by hydrophobic repeats can be envisaged. The same domain is necessary and sufficient to promote specific interaction in vivo, as assayed by the yeast two-hybrid assay. Moreover, an ii? vitro interaction with some SR proteins was also observed. These observations suggest that diverse and specific protein-protein interactions might contribute to the different functions of the hnRNP A1 protein in mRNA maturation. (C) 1996 Academic Press Limited [References: 57]
机译：异质核核糖核蛋白（hnRNPs）是丰富的核多肽，最有可能参与了mRNA前加工的不同步骤。蛋白A1（34 kDa）是hnRNP家族的重要成员，似乎通过调节RNA二级结构并在剪接位点选择和外显子跳过/包含中拮抗某些剪接因子（SR蛋白）起作用。还已经提出了A1在RNA的核质运输中的作用。这些活性可能不仅取决于蛋白质的RNA结合特性，还取决于特定的蛋白质-蛋白质相互作用。在这里，我们报告说，A1确实可以在体外与其自身选择性地相互作用。与其他hnRNP基本的“核心”蛋白。这种选择性结合仅由富含甘氨酸的C-末端结构域介导，其中可以设想由疏水性重复构成的新的蛋白质结合基序。如通过酵母双杂交测定法所测定的，相同的结构域是必需的并且足以促进体内特异性相互作用。而且，ii？还观察到了与某些SR蛋白的体外相互作用。这些观察结果表明，多种多样且特定的蛋白质-蛋白质相互作用可能有助于hnRNP A1蛋白质在mRNA成熟中的不同功能。 （C）1996 Academic Press Limited [参考号：57]

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