Analysis of the Murine All-1 Gene Reveals Conserved Domains with Human ALL-1 and Identifies a Motif Shared with DNA Methyltransferases

• Published in: Proceedings of the National Academy of Sciences - PNAS 1993-07, Vol.90 (13), p.6350-6354
• Main Authors: Ma, Qing, Alder, Hansjuerg, Nelson, Kelly K., Chatterjee, Devjani, Gu, Yansong, Nakamura, Tatsuya, Canaani, Eli, Croce, Carlo M., Siracusa, Linda D., Buchberg, Arthur M.
• Format: Article
• Language: English
• Subjects: Alternative Splicing; Amino Acid Sequence; Animals; Base Sequence; Biological and medical sciences; Chromosome Mapping; Chromosomes, Human, Pair 11; Complementary DNA; Conserved Sequence; DNA; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; Fundamental and applied biological sciences. Psychology; Genes; Genes. Genome; Genetic loci; Genetic mutation; Genetics; Genomics; Histone-Lysine N-Methyltransferase; Humans; Leukemia; Medical research; Methyltransferases - chemistry; Mice; Mice, Inbred C57BL; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Myeloid-Lymphoid Leukemia Protein; O-Methylguanine-DNA Methyltransferase; Oncogenes; Open Reading Frames; Precursor Cell Lymphoblastic Leukemia-Lymphoma - genetics; Proteins; Proto-Oncogenes; Regional identity; Rodents; Transcription Factors; Zinc; Zinc Fingers
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.90.13.6350

A series of translocation break points found in a subset of human acute leukemias have one of the breaks on human chromosome 11q23. This region has recently been cloned and a large gene, ALL-1, with homology to the Drosophila trithorax gene has been identified. This paper describes the cloning, sequencing, and mapping of the mouse homolog of ALL-1. We have found a motif present in All-1 that shows homology to the zinc-binding domain of DNA (cytosine-5) methyltransferases (EC 2.1.1.63). Sequence analysis of the murine All-1 gene has identified distinct regions of homology with the human ALL-1 gene; these highly conserved domains may define regions of functional significance in mammals. In addition, we have identified alternatively spliced forms of All-1 within one of the zinc-finger domains, suggesting that there may be different targets and/or functions for All-1 proteins. Finally, we report that All-1 resides in the proximal portion of mouse chromosome 9 and is a candidate for a mutation that results in skeletal transformations during embryonic development.