Phosphorylation of an N-terminal motif enhances DNA-binding activity of the human SRY protein
| Autor: | Philippe Berta, Brigitte Moniot, Marion Desclozeaux, Francis Poulat, Brigitte Boizet, Philippe Jay, Patric Turowski, Jean-Paul Capony, Pascal de Santa Barbara, Catherine Méjean |
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| Rok vydání: | 1998 |
| Předmět: |
Molecular Sequence Data
Nuclear Proteins Cell Biology DNA Biology Phosphoproteins Biochemistry In vitro Sex-Determining Region Y Protein Cell Line Serine DNA-Binding Proteins Testis determining factor In vivo Transcriptional regulation Phosphorylation Humans Amino Acid Sequence Protein kinase A Molecular Biology Gene Protein Binding Transcription Factors |
| Zdroj: | The Journal of biological chemistry. 273(14) |
| ISSN: | 0021-9258 |
| Popis: | Of the several strategies that eukaryotes have evolved to modulate transcription factor activity, phosphorylation is regarded as one of the major mechanisms in signal-dependent transcriptional control. To conclusively demonstrate that the human sex-determining gene SRY is affected by such a post-translational control mechanism, we have analyzed its phosphorylation status in living cells. In the present study, we show that the cyclic AMP-dependent protein kinase (PKA) phosphorylates the human SRY protein in vitro as well as in vivo on serine residues located in the N-terminal part of the protein. This phosphorylation event was shown to positively regulate SRY DNA-binding activity and to enhance the ability of SRY to inhibit a basal promoter activity located downstream of an SRY DNA-binding site concatamer. Together these results strongly support the hypothesis that human SRY is a natural substrate for PKA in vivo and that this phosphorylation significantly modulates its major activity, DNA-binding, thereby possibly altering its biological function. |
| Databáze: | OpenAIRE |
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