| First Author | Witthuhn BA | Year | 1996 |
| Journal | Mol Immunol | Volume | 33 |
| Issue | 10 | Pages | 881-90 |
| PubMed ID | 8845020 | Mgi Jnum | J:35615 |
| Mgi Id | MGI:83062 | Doi | 10.1016/0161-5890(96)84614-1 |
| Citation | Witthuhn BA, et al. (1996) Isolation and characterization of the rat beta-subunit gene of the high affinity receptor for immunoglobulin E. Mol Immunol 33(10):881-90 |
| abstractText | 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. |
