hnRNP G: sequence and characterization of a glycosylated RNA-binding protein.
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.
Soulard
M
M
INSERM U-301, Institut de Génétique Moléculaire, Paris, France.
Della Valle
V
V
Siomi
M C
MC
Piñol-Roma
S
S
Codogno
P
P
Bauvy
C
C
Bellini
M
M
Lacroix
J C
JC
Monod
G
G
Dreyfuss
G
G
D000117:Acetylglucosamine / Q000032:analysis; D000595:Amino Acid Sequence; D000818:Animals; D002875:Chromosomes; D003001:Cloning, Molecular; D016895:Culture Media, Serum-Free; D018076:DNA, Complementary; D006031:Glycosylation; D006367:HeLa Cells; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D006801:Humans; D008969:Molecular Sequence Data; D009865:Oocytes; D010999:Pleurodeles; D012313:RNA / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D016895:Culture Media, Serum-Free; D018076:DNA, Complementary; D034441:Heterogeneous-Nuclear Ribonucleoproteins; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; D012313:RNA; D000117:Acetylglucosamine