Soulard M, Della Valle V, Siomi M C, Piñol-Roma S, Codogno P, Bauvy C, Bellini M, Lacroix J C, Monod G, Dreyfuss G
INSERM U-301, Institut de Génétique Moléculaire, Paris, France.
Nucleic Acids Res. 1993 Sep 11;21(18):4210-7. doi: 10.1093/nar/21.18.4210.
The autoantigen p43 is a nuclear protein initially identified with autoantibodies from dogs with a lupus-like syndrome. Here we show that p43 is an RNA-binding protein, and identify it as hnRNP G, a previously described component of heterogeneous nuclear ribonucleoprotein complexes. We demonstrate that p43/hnRNP G is glycosylated, and identify the modification as O-linked N-acetylglucosamine. A full-length cDNA clone for hnRNP G has been isolated and sequenced, and the predicted amino acid sequence for hnRNP G shows that it contains one RNP-consensus RNA binding domain (RBD) at the amino terminus and a carboxyl domain rich in serines, arginines and glycines. The RBD of human hnRNP G shows striking similarities with the RBDs of several plant RNA-binding proteins.
自身抗原p43是一种核蛋白,最初是在患有狼疮样综合征的犬类自身抗体中被鉴定出来的。在此我们表明,p43是一种RNA结合蛋白,并将其鉴定为hnRNP G,这是一种先前已描述的不均一核核糖核蛋白复合物的组分。我们证明p43/hnRNP G是糖基化的,并确定这种修饰为O-连接的N-乙酰葡糖胺。已分离并测序了hnRNP G的全长cDNA克隆,hnRNP G的预测氨基酸序列表明,它在氨基末端包含一个RNP一致RNA结合结构域(RBD)和一个富含丝氨酸、精氨酸和甘氨酸的羧基结构域。人hnRNP G的RBD与几种植物RNA结合蛋白的RBD具有显著相似性。