| Literature DB >> 7692398 |
M Soulard1, V Della Valle, M C Siomi, S Piñol-Roma, P Codogno, C Bauvy, M Bellini, J C Lacroix, G Monod, G Dreyfuss.
Abstract
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.Entities:
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Year: 1993 PMID: 7692398 PMCID: PMC310052 DOI: 10.1093/nar/21.18.4210
Source DB: PubMed Journal: Nucleic Acids Res ISSN: 0305-1048 Impact factor: 16.971