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

Nucleic Acids Res. 1993 Sep 11;21(18):4210-7. doi: 10.1093/nar/21.18.4210.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylglucosamine / analysis
  • Amino Acid Sequence
  • Animals
  • Chromosomes
  • Cloning, Molecular
  • Culture Media, Serum-Free
  • DNA, Complementary
  • Glycosylation
  • HeLa Cells
  • Heterogeneous-Nuclear Ribonucleoproteins
  • Humans
  • Molecular Sequence Data
  • Oocytes
  • Pleurodeles
  • RNA / metabolism
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / metabolism
  • Ribonucleoproteins / chemistry*
  • Ribonucleoproteins / metabolism
  • Sequence Homology, Amino Acid

Substances

  • Culture Media, Serum-Free
  • DNA, Complementary
  • Heterogeneous-Nuclear Ribonucleoproteins
  • RNA-Binding Proteins
  • Ribonucleoproteins
  • RNA
  • Acetylglucosamine

Associated data

  • GENBANK/Z23064