HNRNP-G - SEQUENCE AND CHARACTERIZATION OF A GLYCOSYLATED RNA-BINDING PROTEIN

被引:140
作者
SOULARD, M
DELLAVALLE, V
SIOMI, MC
PINOLROMA, S
CODOGNO, P
BAUVY, C
BELLINI, M
LACROIX, JC
MONOD, G
DREYFUSS, G
LARSEN, CJ
机构
[1] INST GENET MOLEC,INSERM,U301,27 RUE J DODU,F-75010 PARIS,FRANCE
[2] UNIV PENN,SCH MED,HOWARD HUGHES MED INST,DEPT BIOCHEM & BIOPHYS,PHILADELPHIA,PA 19104
[3] UNIV PARIS 07,INSERM,U239,F-75018 PARIS,FRANCE
[4] UNIV PARIS 06,GENET DEV LAB,F-75230 PARIS 05,FRANCE
关键词
D O I
10.1093/nar/21.18.4210
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:4210 / 4217
页数:8
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