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Cloning and characterization of hGMEB1, a novel glucocorticoid modulatory element binding protein
Author(s) -
Thériault Jimmy R,
Charette Steve J,
Lambert Herman,
Landry Jacques
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00634-1
Subject(s) - immunoprecipitation , glucocorticoid receptor , complementary dna , biology , microbiology and biotechnology , hsp27 , heat shock protein , binding protein , glucocorticoid , biochemistry , hsp70 , gene , endocrinology
A 21‐bp element called glucocorticoid modulatory element (GME) modulates the glucocorticoid receptor‐mediated responses via the binding of an as yet poorly characterized trans ‐acting 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.