A murine ATFa-associated factor with transcriptional repressing activity
| Autor: | De Graeve F, Bruno Chatton, A Bahr, Claude Kedinger |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Cancer Research
DNA Complementary Transcription Genetic Molecular Sequence Data RNA polymerase II Biology CREB Embryonic and Fetal Development Mice Transcription Factors TFII Transcription (biology) Genetics Animals Humans Amino Acid Sequence Cyclic AMP Response Element-Binding Protein Molecular Biology Transcription factor Adenosine Triphosphatases Cell Nucleus Base Sequence General transcription factor Molecular biology Repressor Proteins Transcription Factor TFIIH COS Cells Transcription factor II H biology.protein RNA Polymerase II Transcription factor II E Transcription Factors |
| Zdroj: | Oncogene. 19:1807-1819 |
| ISSN: | 1476-5594 0950-9232 |
| DOI: | 10.1038/sj.onc.1203492 |
| Popis: | The ATFa proteins, which are members of the CREB/ATF family of transcription factors, have previously been shown to interact with the adenovirus E1a oncoprotein and to mediate its transcriptional activity; they heterodimerize with Jun, Fos or related transcription factors, possibly altering their DNA-binding specificity; they also stably bind JNK2, a stress-induced protein kinase. Here we report the identification and characterization of a novel protein isolated in a yeast two-hybrid screen using the N-terminal half of ATFa as a bait. This 1306-residue protein (mAM, for mouse ATFa-associated Modulator) is rather acidic (pHi 4.5) and contains high proportions of Ser/Thr (21%) and Pro (11%) residues. It colocalizes and interacts with ATFa in mammalian cells, contains a bipartite nuclear localization signal and possesses an ATPase activity. Transfection experiments show that mAM is able to downregulate transcriptional activity, in an ATPase-independent manner. Our results indicate that mAM interacts with several components of the basal transcription machinery (TFIIE and TFIIH), including RNAPII itself. Together, these findings suggest that mAM may be involved in the fine-tuning of ATFa-regulated gene expression, by interfering with the assembly or stability of specific preinitiation transcription complexes. |
| Databáze: | OpenAIRE |
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