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Beck, BD, Park, SJ, Lee, YJ, Roman, Y, Hromas, RA and Lee, SH (2008) Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair. J. Biol. Chem. 283:9023-30
Metnase, also known as SETMAR, is a SET and transposase fusion protein with an undefined role in mammalian DNA repair. The SET domain is responsible for histone lysine methyltransferase activity at histone 3 K4 and K36, whereas the transposase domain possesses 5'-terminal inverted repeat (TIR)-specific DNA binding, DNA looping, and DNA cleavage activities. Although the transposase domain is essential for Metnase function in DNA repair, it is not clear how a protein with sequence-specific DNA binding activity plays a role in DNA repair. Here, we show that human homolog of the ScPSO4/PRP19 (hPso4) forms a stable complex with Metnase on both TIR and non-TIR DNA. The transposase domain essential for Metnase-TIR interaction is not sufficient for its interaction with non-TIR DNA in the presence of hPso4. In vivo, hPso4 is induced and co-localized with Metnase following ionizing radiation treatment. Cells treated with hPso4-siRNA failed to show Metnase localization at DSB sites and Metnase-mediated stimulation of DNA end joining coupled to genomic integration, suggesting that hPso4 is necessary to bring Metnase to the DSB sites for its function(s) in DNA repair.
Cell Line; DNA Breaks, Double-Stranded; DNA Repair/physiology; DNA Repair Enzymes/antagonists & inhibitors; DNA Repair Enzymes/genetics; DNA Repair Enzymes/metabolism; DNA-Binding Proteins/antagonists & inhibitors; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Histone-Lysine N-Methyltransferase/genetics; Histone-Lysine N-Methyltransferase/metabolism; Histones/metabolism; Humans; Nuclear Proteins/antagonists & inhibitors; Nuclear Proteins/genetics; Nuclear Proteins/metabolism; Protein Structure, Tertiary/physiology; RNA, Small Interfering/genetics; Terminal Repeat Sequences/physiology