| First Author | Ogawa H | Year | 2003 |
| Journal | Genes Cells | Volume | 8 |
| Issue | 4 | Pages | 325-39 |
| PubMed ID | 12653961 | Mgi Jnum | J:85111 |
| Mgi Id | MGI:2671970 | Doi | 10.1046/j.1365-2443.2003.00636.x |
| Citation | Ogawa H, et al. (2003) A SWI2/SNF2-type ATPase/helicase protein, mDomino, interacts with myeloid zinc finger protein 2A (MZF-2A) to regulate its transcriptional activity. Genes Cells 8(4):325-39 |
| abstractText | BACKGROUND: The myeloid zinc finger protein 2A (MZF-2A) is a Kruppel-type C2H2 zinc finger transcription factor expressed in myeloid cells and involved in the growth, differentiation and tumorigenesis of myeloid progenitors. Previously we identified a 180 amino acid domain in MZF-2A which is responsible for the transcriptional activation of MZF-2A. To understand the mechanism of the MZF-2A-dependent transcriptional activation, we screened for molecules that interact with the transactivation domain (TAD) of MZF-2A. RESULTS: By using the yeast Ras recruitment two-hybrid screening, we identified a novel SWI2/SNF2-related protein, termed mammalian Domino (mDomino), as an MZF-2A-binding partner. The mDomino protein, which shows a marked similarity to the Drosophila Domino protein, contains a SWI2/SNF2-type ATPase/helicase domain, a SANT domain, and a glutamine-rich (Q-rich) domain. The C-terminal Q-rich domain of mDomino physically associates with the TAD of MZF-2A in mammalian cells as well as in yeast. Expression of the mDomino Q-rich domain, together with MZF-2A in myeloid LGM-1 cells, enhanced the MZF-2A-mediated activation of a reporter gene. CONCLUSIONS: These results strongly suggest that an ATP-dependent chromatin-remodelling complex containing mDomino interacts with MZF-2A to regulate gene expression in myeloid cells. |
