Isolation and characterization of the rat beta-subunit gene of the high affinity receptor for immunoglobulin E.
The high affinity receptor for IgE, which mediates allergic reactions, is found exclusively on mast cells, basophils and epidermal Langerhans cells. It is composed of an alpha, beta and two gamma-polypeptide chains, inserted as a complex into the plasma membrane. The alpha and beta-subunits are produced only by these cell types. This work describes the isolation and characterization of the gene which encodes the rat beta-subunit. The single copy gene spans a 9 kbp region of DNA and is composed of seven exons and six introns. Transcriptional initiation begins from a single site, which is preceded by a very unique, putative transcriptional consensus sequence, the GATA box. Analysis of the 5'-region, upstream of exon 1, also reveals a unique sequence bias and a collection of repeating elements, suggesting several other potential transcriptional cis-control elements. The origins of the two, previously reported, different beta-subunit transcripts result from the same start site of this gene, but use an alternative RNA processing mechanism involving exon 3.
Witthuhn
B A
BA
Texas Tech University Health Sciences Center, Department of Cell Biology and Biochemistry, Lubbock 79430, USA.
Faust
C
C
D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary; D015698:Genomic Library; D006801:Humans; D008969:Molecular Sequence Data; D016133:Polymerase Chain Reaction; D051381:Rats; D017207:Rats, Sprague-Dawley; D017455:Receptors, IgE / Q000235:genetics*; D016415:Sequence Alignment; D016385:TATA Box
D018076:DNA, Complementary; D017455:Receptors, IgE