Literature DB >> 7692398

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

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.

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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


  41 in total

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Journal:  Biochemistry       Date:  1988-07-12       Impact factor: 3.162

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Journal:  J Cell Biol       Date:  1987-02       Impact factor: 10.539

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9.  Degeneracy in human multicopy RBM (YRRM), a candidate spermatogenesis gene.

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