Biochemical analyses of the AF10 protein: the extended LAP/PHD-finger mediates oligomerisation
| Autor: | B, Linder, R, Newman, L K, Jones, S, Debernardi, B D, Young, P, Freemont, C P, Verrijzer, V, Saha |
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| Rok vydání: | 2000 |
| Předmět: |
Cell Nucleus
Recombinant Fusion Proteins Amino Acid Motifs Molecular Sequence Data Nuclear Localization Signals DNA Single-Stranded Biological Transport DNA-Binding Proteins Molecular Weight Microscopy Electron Cross-Linking Reagents Leukemia Myeloid Mutation Chromatography Gel Humans Nucleic Acid Conformation Amino Acid Sequence Sequence Alignment Conserved Sequence HeLa Cells Protein Binding Transcription Factors |
| Zdroj: | Journal of molecular biology. 299(2) |
| ISSN: | 0022-2836 |
| Popis: | Leukaemogenesis correlates with alterations in chromatin structure brought about by the gain or loss of interactive domains from regulatory factors that are disrupted by chromosomal translocations. The gene MLL, a target of such translocation events, forms chimaeric fusion products with a variety of partner genes. While MLL appears to be involved in chromatin-mediated gene regulation, the functions of its partner genes are largely speculative. We report the biochemical analysis of the MLL partner gene AF10 and its possible role in leukaemogenesis. AF10 has been reported to be re-arranged with genes other than MLL leading to the same phenotype, a myeloid leukaemia. We have identified a novel protein-protein interaction motif in the AF10 protein comprising the extended LAP/PHD-finger. This domain mediates homo-oligomerisation of recombinant AF10 and is conserved in several proteins, including MLL itself. AF10 binds cruciform DNA via a specific interaction with an AT-hook motif and is localised to the nucleus by a defined bipartite nuclear localisation signal in the N-terminal region. |
| Databáze: | OpenAIRE |
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