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


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
Issue number18
StatePublished - Sep 11 1993
Externally publishedYes

ASJC Scopus subject areas

  • Genetics


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