Self-association of the SET domains of human ALL-1 and of Drosophila TRITHORAX and ASH1 proteins
Oncogene(2000)
Abstract
The human ALL-1 gene is involved in acute leukemia through gene fusions, partial tandem duplications or a specific deletion. Several sequence motifs within the ALL-1 protein, such as the SET domain, PHD fingers and the region with homology to DNA methyl transferase are shared with other proteins involved in transcription regulation through chromatin alterations. However, the function of these motifs is still not clear. Studying ALL-1 presents an additional challenge because the gene is the human homologue of Drosophila trithorax . The latter is a member of the trithorax-Polycomb gene family which acts to determine the body pattern of Drosophila by maintaining expression or repression of the Antennapedia-bithorax homeotic gene complex. Here we apply yeast two hybrid methodology, in vivo immunoprecipitation and in vitro `pull down' techniques to show self association of the SET motifs of ALL-1, TRITHORAX and ASH1 proteins ( Drosophila ASH1 is encoded by a trithorax -group gene). Point mutations in evolutionary conserved residues of TRITHORAX SET, abolish the interaction. SET–SET interactions might act in integrating the activity of ALL-1 (TRX and ASH1) protein molecules, simultaneously positioned at different maintenance elements and directing expression of the same or different target genes.
MoreTranslated text
Key words
SET domain,oligomerization,chromatin alterations
AI Read Science
Must-Reading Tree
Example
![](https://originalfileserver.aminer.cn/sys/aminer/pubs/mrt_preview.jpeg)
Generate MRT to find the research sequence of this paper
Chat Paper
Summary is being generated by the instructions you defined