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. 1993 Sep 11;21(18):4210–4217. doi: 10.1093/nar/21.18.4210

hnRNP G: sequence and characterization of a glycosylated RNA-binding protein.

M Soulard 1, V Della Valle 1, M C Siomi 1, S Piñol-Roma 1, P Codogno 1, C Bauvy 1, M Bellini 1, J C Lacroix 1, G Monod 1, G Dreyfuss 1
PMCID: PMC310052  PMID: 7692398

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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Selected References

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