Insertion of an amino acid in the DNA-binding domain of the glucocorticoid receptor as a result of alternative splicing.
When the human glucocorticoid receptor (GR) was first sequenced, a predominant form (GRalpha) and a minor variant (GRbeta) were identified. In the present communication, we describe a new variant of the glucocorticoid receptor (GRgamma) in which, as a result of alternative splicing, three bases are retained from the intron separating exons 3 and 4. These three bases code for an additional amino acid (arginine) in the DNA binding domain of the receptor. Insertion of arginine at this site has previously been shown to decrease transcriptional activation by the GR to 48% that of GRalpha. Analysis of cDNA from different tissues shows that the novel form is widely expressed at a relatively high level (between 3.8 and 8.7% of total GR).
Rivers
C
C
Division of Medicine, University of Bristol, UK.
Levy
A
A
Hancock
J
J
Lightman
S
S
Norman
M
M
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D018076:DNA, Complementary / Q000032:analysis; D005091:Exons; D014644:Genetic Variation; D006801:Humans; D011965:Receptors, Glucocorticoid / Q000737:chemistry* / Q000235:genetics*
D018076:DNA, Complementary; D011965:Receptors, Glucocorticoid; D004247:DNA; D001120:Arginine