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PMID:20620605

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Citation

Wray, J, Williamson, EA, Chester, S, Farrington, J, Sterk, R, Weinstock, DM, Jasin, M, Lee, SH, Nickoloff, JA and Hromas, R (2010) The transposase domain protein Metnase/SETMAR suppresses chromosomal translocations. Cancer Genet. Cytogenet. 200:184-90

Abstract

Chromosomal translocations are common in leukemia, but little is known about their mechanism. Metnase (also termed SETMAR) is a fusion of a histone methylase and transposase protein that arose specifically in primates. Transposases were thought to be extinct in primates because they would mediate deleterious DNA movement. In primates, Metnase interacts with DNA Ligase IV (Lig IV) and promotes nonhomologous end-joining (NHEJ) DNA repair. We show here that the primate-specific protein Metnase can also enhance NHEJ in murine cells and can also interact with murine Lig IV, indicating that it integrated into the preexisting NHEJ pathway after its development in primates. Significantly, expressing Metnase in murine cells significantly reduces chromosomal translocations. We propose that the fusion of the histone methylase SET domain and the transposase domain in the anthropoid lineage to form primate Metnase promotes accurate intrachromosomal NHEJ and thereby suppresses interchromosomal translocations. Metnase may have been selected for because it has a function opposing transposases and may thus play a key role in suppressing translocations that underlie oncogenicity.

Links

PubMed PMC2904321 Online version:10.1016/j.cancergencyto.2010.04.011

Keywords

Animals; DNA Ligases/physiology; DNA Repair; DNA-Binding Proteins/physiology; Histone-Lysine N-Methyltransferase/physiology; Mice; NIH 3T3 Cells; Recombinant Fusion Proteins/physiology; Translocation, Genetic; Transposases/physiology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:SETMR

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8BTF7

F

Seeded From UniProt

complete

MOUSE:DNLI4

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q53H47

F

Seeded From UniProt

complete

HUMAN:SETMR

involved_in

GO:2001251: negative regulation of chromosome organization

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:SETMR

enables

GO:0004519: endonuclease activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:SETMR

involved_in

GO:2001034: positive regulation of double-strand break repair via nonhomologous end joining

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete


See also

References

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