Nucleic Acids Research, 1993, Vol. 21, No. 18 4210-4217
© 1993
MOLECULAR BIOLOGY |
hnRNP G: sequence and characterization of a glycosylated RNA-binding protein
INSERM U-301, Institut de Geèneètique Moleèculaire 27 rue J.Dodu, 75010 Paris, France 1Howard Hughes Medical Institue, Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania PA 19104-6148 USA 2INSERM U-239 Faculteè de Meèdecine Xavier Bichat 16 rue H. Huchard, 75018 Paris 3Laboratoire de Geèneètoque du Deèveloppement, Universite P.et M.currie Pl.Jussieu, 75005 Paris, France
*To whom correspondence should be addressed
Received June 14, 1993. Revised September 28, 1993. Accepted September 28, 1993.
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.
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