title: Autokinase activity of alpha-crystallin inhibits its specific interaction with the DOTIS element in the murine gamma D/E/F-crystallin promoter in vitro.
abstract: In a previous report we demonstrated the in vitro interaction of alpha-crystallin with an element downstream of the transcriptional initiation site (DOTIS) of the murine gamma E-crystallin promoter (Pietrowski et al., 1994, Gene 144, 171-178). The aim of the present study was to investigate the influence of phosphorylation on this particular interaction. We could demonstrate that the autophosphorylation of alpha-crystallin leads to a complete loss of interaction with the DOTIS element, however, PKA-dependent phosphorylation of alpha-crystallin is without effect on the interaction. It is hypothesized that the autophosphorylation of alpha-crystallin might be involved in regulatory mechanisms of the murine gamma D/E/F-crystallin gene expression.
authors.affiliation: GSF-National Research Center for Environment and Health, Institute of Mammalian Genetics, Neuherberg, Germany.
authors.forename: D
authors.initials: D
authors.lastname: Pietrowski
authors.forename: J
authors.initials: J
authors.lastname: Graw
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003459:Crystallins / Q000235:genetics*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000737:chemistry; D005786:Gene Expression Regulation / Q000235:genetics*; D051379:Mice; D011401:Promoter Regions, Genetic / Q000235:genetics; D011494:Protein Kinases / Q000235:genetics*; D014158:Transcription, Genetic
chemical_list: D003459:Crystallins; D011494:Protein Kinases; C091973:autophosphorylation-dependent multifunctional protein kinase; D017868:Cyclic AMP-Dependent Protein Kinases