hnRNP G: sequence and characterization of a glycosylated RNA-binding protein
Authors:
- Veèronique Della ValleVVVeèronique Della Valle
- Mikkiko C. SiomiMSMikkiko C. Siomi
- Serafin Pin`oL-RomaSPSerafin Pin`oL-Roma
- Patrice CodognoPCPatrice Codogno
- Chantal BauvyCBChantal Bauvy
- Michel BelliniMBMichel Bellini
- Jean-Claude LacroixJLJean-Claude Lacroix
- Guillaume MonodGMGuillaume Monod
- Gidden DreyfussGDGidden Dreyfuss
- Christian-Jacques LarsenCLChristian-Jacques Larsen
- 1 January 1993
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 21 (18) , 4210-4217
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.Keywords
This publication has 39 references indexed in Scilit:
- O-glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulationCell, 1988
- Identification of carbohydrate binding protein 35 in heterogeneous nuclear ribonucleoprotein complexBiochemistry, 1988
- A gene induced by the plant hormone abscisic acid in response to water stress encodes a glycine-rich proteinNature, 1988
- cDNA cloning of human hnRNP protein Al reveals the existence of multiple mRNA isoformsNucleic Acids Research, 1988
- Immunopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA-binding proteins.Genes & Development, 1988
- Primary structure of human nuclear ribonucleoprotein particle C proteins: conservation of sequence and domain structures in heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins.Molecular and Cellular Biology, 1987
- Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores.Journal of Cell Biology, 1987
- Structure and Function of Nuclear and Cytoplasmic Ribonucleoprotein ParticlesAnnual Review of Cell Biology, 1986
- Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomesCell, 1986
- CELL-SURFACE GLYCOPEPTIDES FROM HUMAN INTESTINAL EPITHELIAL-CELL LINES DERIVED FROM NORMAL COLON AND COLON ADENOCARCINOMAS1985