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PMID: 8327517 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Analysis of the murine All-1 gene reveals conserved domains with human ALL-1 and identifies a motif shared with DNA methyltransferases.

Ma Q, Alder H, Nelson KK, Chatterjee D, Gu Y, Nakamura T, Canaani E, Croce CM, Siracusa LD, Buchberg AM

Abstract

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.

MeSH Terms
Alternative Splicing Amino Acid Sequence Animals Base Sequence Chromosome Mapping Chromosomes, Human, Pair 11 Conserved Sequence DNA-Binding Proteins/chemistry,genetics Histone-Lysine N-Methyltransferase Humans Methyltransferases/chemistry Mice Mice, Inbred C57BL Molecular Sequence Data Myeloid-Lymphoid Leukemia Protein O(6)-Methylguanine-DNA Methyltransferase Oncogenes Open Reading Frames Precursor Cell Lymphoblastic Leukemia-Lymphoma/genetics Proto-Oncogenes Transcription Factors Zinc Fingers
Chemicals
DNA-Binding Proteins KMT2A protein, human Transcription Factors Myeloid-Lymphoid Leukemia Protein Methyltransferases Histone-Lysine N-Methyltransferase Kmt2a protein, mouse O(6)-Methylguanine-DNA Methyltransferase
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Ma Q
Jefferson Cancer Institute, Jefferson Medical College, Philadelphia, PA 19107-5541.
Alder H
Nelson K K
Chatterjee D
Gu Y
Nakamura T
Canaani E
Croce C M
Siracusa L D
Buchberg A M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1993-07-01
Pages
6350-4
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC46926
Subset
IM
Grants
NCI NIH HHS · CA39860 · United States
NCI NIH HHS · CA58586 · United States
Databases
GENBANK
L17069
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