Skip to main navigation Skip to search Skip to main content

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

  • Michel Soulard
  • , Veèronique Della Valle
  • , Mikkiko C. Siomi
  • , Serafin Pinol-roma
  • , Patrice Codogno
  • , Chantal Bauvy
  • , Michel Bellini
  • , Jean claude Lacroix
  • , Guillaume Monod
  • , Gidden Dreyfuss
  • , Christian jacques Larsen

Research output: Contribution to journalArticlepeer-review

Abstract

The autoantlgen p43 is a nuclear protein initially identified with autoantibodles from dogs with a lupuslike syndrome. Here we show that p43 Is an RNAblnding protein, and identify it as hnRNP G, a previously described component of heterogeneous nuclear ribonucleoproteln complexes. We demonstrate that p43/hnRNP G Is glycosylated, and identify the modification as O-linked N-acetylglucosamine. A fulllength cDNA clone for hnRNP G has been isolated and sequenced, and the predicted amlno acid sequence for hnRNP G shows that It contains one RNP-consensus RNA binding domain (RBD) at the amlno terminus and a carboxyl domain rich In serines, arglnines and glyclnes. The RBD of human hnRNP G shows striking similarities with the RBDs of several plant RNA-blndlng proteins.

Original languageEnglish (US)
Pages (from-to)4210-4217
Number of pages8
JournalNucleic acids research
Volume21
Issue number18
DOIs
StatePublished - Sep 11 1993
Externally publishedYes

ASJC Scopus subject areas

  • Genetics

Fingerprint

Dive into the research topics of 'hnRNP G: Sequence and characterization of a glycosylated RNA-binding protein'. Together they form a unique fingerprint.

Cite this