PMID- 10656681 OWN - NLM STAT- MEDLINE DCOM- 20000210 LR - 20191126 IS - 0950-9232 (Print) IS - 0950-9232 (Linking) VI - 19 IP - 3 DP - 2000 Jan 20 TI - Self-association of the SET domains of human ALL-1 and of Drosophila TRITHORAX and ASH1 proteins. PG - 351-7 AB - 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. FAU - Rozovskaia, T AU - Rozovskaia T AD - Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot, Israel. FAU - Rozenblatt-Rosen, O AU - Rozenblatt-Rosen O FAU - Sedkov, Y AU - Sedkov Y FAU - Burakov, D AU - Burakov D FAU - Yano, T AU - Yano T FAU - Nakamura, T AU - Nakamura T FAU - Petruck, S AU - Petruck S FAU - Ben-Simchon, L AU - Ben-Simchon L FAU - Croce, C M AU - Croce CM FAU - Mazo, A AU - Mazo A FAU - Canaani, E AU - Canaani E LA - eng GR - CA 50507/CA/NCI NIH HHS/United States PT - Journal Article PT - Research Support, Non-U.S. Gov't PT - Research Support, U.S. Gov't, P.H.S. PL - England TA - Oncogene JT - Oncogene JID - 8711562 RN - 0 (ASH1 protein, Drosophila) RN - 0 (Chromatin) RN - 0 (DNA-Binding Proteins) RN - 0 (Drosophila Proteins) RN - 0 (KMT2A protein, human) RN - 0 (Transcription Factors) RN - 0 (Trl protein, Drosophila) RN - 149025-06-9 (Myeloid-Lymphoid Leukemia Protein) RN - EC 2.1.1.43 (ASH1L protein, human) RN - EC 2.1.1.43 (Histone-Lysine N-Methyltransferase) SB - IM MH - Amino Acid Motifs MH - Amino Acid Sequence MH - Animals MH - Chromatin/chemistry MH - Conserved Sequence MH - DNA-Binding Proteins/*chemistry MH - Drosophila MH - *Drosophila Proteins MH - Histone-Lysine N-Methyltransferase MH - Humans MH - Molecular Sequence Data MH - Myeloid-Lymphoid Leukemia Protein MH - Point Mutation MH - Precipitin Tests MH - *Proto-Oncogenes MH - Transcription Factors/*chemistry EDAT- 2000/02/03 00:00 MHDA- 2000/02/03 00:01 CRDT- 2000/02/03 00:00 PHST- 2000/02/03 00:00 [pubmed] PHST- 2000/02/03 00:01 [medline] PHST- 2000/02/03 00:00 [entrez] AID - 10.1038/sj.onc.1203307 [doi] PST - ppublish SO - Oncogene. 2000 Jan 20;19(3):351-7. doi: 10.1038/sj.onc.1203307.