Evidence for two structurally related progesterone receptors in chick oviduct cytosol

FEBS Letters

Harry, Paula¹  Chambon, Pierre¹  Gronemeyer, Hinrich¹ 

[1] Laboratoire de Génétique Moléculaire des Eucaryotes du CNRS, U. 184 de Biologie Moléculaire et de Génie Génétique de l'INSERM, Faculté de Médecine, 11 Rue Humann, 67085 Strasbourg Cedex, France

关键词: Steroid hormone receptor Peptide mapping Photoaffinity labelling Hormone binding domain;   

DOI  :  10.1016/0014-5793(83)80514-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The existence of two progesterone receptor forms present in crude cytosol of chick oviduct has been demonstrated by photoaffinity labelling using [³H]R5020. On SDS—polyacrylamide gels these two forms exhibit app. M _r-values of 79 000 and 109 000 corresponding to the progesterone receptor forms A and B. Peptide maps of photoaffinity-labelled steroid receptors have been established by limited proteolysis with α-chymotrypsin. The peptide map obtained for chick oviduct cytosol progesterone receptor crosslinked with [³H]R5020 proved to be the sum of peptides obtained from partially purified preparations of forms A and B. The peptide maps of both progesterone receptor forms were identical for peptides below the M _r-value of form A, indicating extensive homology of the two forms. A significantly different peptide pattern was observed for the rat liver glucocorticoid receptor crosslinked with [³H]triamcinolone acetonide. Prolonged proteolysis with chymotrypsin gave rise to peptides with M _r-values of 6000 and 10 000 from the hormone-binding domain of progesterone and glucocorticoid receptors, respectively.

【 授权许可】

Unknown