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hnRNP G: sequence and characterization of a glycosylated RNA-binding protein.
Authors:M Soulard, V Della Valle, M C Siomi, S Pi  ol-Roma, P Codogno, C Bauvy, M Bellini, J C Lacroix, G Monod,   G Dreyfuss
Affiliation:M Soulard, V Della Valle, M C Siomi, S Piñol-Roma, P Codogno, C Bauvy, M Bellini, J C Lacroix, G Monod, and 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.
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