| First Author | Thériault JR | Year | 1999 |
| Journal | FEBS Lett | Volume | 452 |
| Issue | 3 | Pages | 170-6 |
| PubMed ID | 10386584 | Mgi Jnum | J:55671 |
| Mgi Id | MGI:1339192 | Doi | 10.1016/s0014-5793(99)00634-1 |
| Citation | Theriault JR, et al. (1999) Cloning and characterization of hGMEB1, a novel glucocorticoid modulatory element binding protein. FEBS Lett 452(3):170-6 |
| abstractText | A 21-bp element called glucocorticoid modulatory element (GME) modulates the glucocorticoid receptor-mediated responses via the binding of an as yet poorly characterized transacting complex of proteins containing the 88-kDa GMEB1 and the 67-kDa GMEB2. Using heat shock protein 27 (HSP27) as bait in the yeast two-hybrid assay, we cloned a 1.83-kb cDNA encoding a novel 573-amino acid protein called human GMEB1 (hGMEB1). hGMEB1 possesses a KDWK domain, contains sequences almost identical (36/38) to three tryptic peptides of rat GMEB1 and shares 38% identity with rat GMEB2. hGMEB1 is ubiquitously expressed as a 85-kDa protein in all cell lines and tissues examined. In vitro translated hGMEB1 bound specifically to GME oligonucleotides yielding a complex of similar size to the complex obtained using rat liver nuclear extracts. Both complexes were supershifted with an antibody specific to hGMEB1. Co-immunoprecipitation experiments confirmed the in vivo interaction of HSP27 with hGMEB1. |
