دورية أكاديمية
Regulatory domains of the A-Myb transcription factor and its interaction with the CBP/p300 adaptor molecules
العنوان: | Regulatory domains of the A-Myb transcription factor and its interaction with the CBP/p300 adaptor molecules |
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المؤلفون: | FACCHINETTI, Valeria, LOFFARELLI, Livio, SCHREEK, Sabine, OELGESCHLÄGER, Michael, LÜSCHER, Bernhard, INTRONA, Martino, GOLAY, Josée |
المصدر: | Biochemical Journal ; volume 324, issue 3, page 729-736 ; ISSN 0264-6021 1470-8728 |
بيانات النشر: | Portland Press Ltd. |
سنة النشر: | 1997 |
الوصف: | The A-Myb transcription factor belongs to the Myb family of oncoproteins and is likely to be involved in the regulation of proliferation and/or differentiation of normal B cells and Burkitt's lymphoma cells. To characterize in detail the domains of A-Myb that regulate its function, we have generated a series of deletion mutants and have investigated their trans-activation potential as well as their DNA-binding activity. Our results have allowed us to delineate the trans-activation domain as well as two separate regulatory regions. The boundaries of the trans-activation domain (amino acid residues 218–319) are centred on a sequence rich in charged amino acids (residues 259–281). A region (residues 320–482) localized immediately downstream of the trans-activation domain and containing a newly identified conserved stretch of 48 residues markedly inhibits specific DNA binding. Finally the last 110 residues of A-Myb (residues 643–752), which include a sequence conserved in all mammalian myb genes (region III), negatively regulate the maximal trans-activation potential of A-Myb. We have also investigated the functional interaction between A-Myb and the nuclear adaptor molecule CBP [cAMP response element-binding protein (CREB)-binding protein]. We demonstrate that CBP synergizes with A-Myb in a dose-dependent fashion, and that this co-operative effect can be inhibited by E1A and can also be observed with the CBP homologue p300. We show that this functional synergism requires the presence of the A-Myb charged sequence and that it involves physical interaction between A-Myb and the CREB-binding domain of CBP. |
نوع الوثيقة: | article in journal/newspaper |
اللغة: | English |
DOI: | 10.1042/bj3240729 |
الإتاحة: | https://doi.org/10.1042/bj3240729Test https://portlandpress.com/biochemj/article-pdf/324/3/729/624784/bj3240729.pdfTest |
رقم الانضمام: | edsbas.CBFF3770 |
قاعدة البيانات: | BASE |
DOI: | 10.1042/bj3240729 |
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