Pax-QNR/Pax-6, a Paired- and Homeobox-Containing Protein, Recognizes Ets Binding Sites and Can Alter the Transactivating Properties of Ets Transcription Factors
| Autor: | Plaza, Serge, Grevin, Delphine, MacLeod, Kay, Stehelin, Dominique, Saule, Simon |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
Homeodomain Proteins
Transcriptional Activation congenital hereditary and neonatal diseases and abnormalities animal structures Binding Sites Base Sequence PAX6 Transcription Factor Proto-Oncogene Proteins c-ets Molecular Sequence Data Quail Article body regions DNA-Binding Proteins Repressor Proteins Mice Proto-Oncogene Proteins embryonic structures Animals Humans Paired Box Transcription Factors sense organs Eye Proteins Cells Cultured Transcription Factors |
| Popis: | We have previously isolated a cDNA clone encoding a protein with a paired- and homeodomain from MC29-transformed quail neuroretina cells that we have termed Pax-QNR. Pax-QNR is homologous to the murine Pax-6, which is mutated in the autosomal dominant mutation small eye (Sey) of the mouse and aniridia in man. The 46 kDa Pax-QNR protein binds specifically to the e5 DNA recognition sequence present upstream of the Drosophila even-skipped gene. The Pax-QNR paired and homeobox domains expressed separately in bacteria are both able to recognize this sequence. The core sequence recognized by the paired domain of Pax genes is TTCC (GGAA), and this sequence is also present in the core recognition site bound specifically by Ets family-encoded proteins. Ets proteins are a family of transcription factors sharing a highly conserved 85 amino acid DNA binding domain. In this article we demonstrate that Pax-QNR/Pax-6 expressed in reticulocyte lysate is able to specifically recognize several Ets binding sites. In addition, we found that the transactivation mediated by the p68c-ets-1 pr p55erg through the Polyomavirus enhancer sequence is specifically inhibited by the p46kDaPax-QNR in transient transfection assay. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|