| First Author | Dmitriev RI | Year | 2007 |
| Journal | Biochem Biophys Res Commun | Volume | 355 |
| Issue | 4 | Pages | 1051-7 |
| PubMed ID | 17335777 | Mgi Jnum | J:120330 |
| Mgi Id | MGI:3706282 | Doi | 10.1016/j.bbrc.2007.02.073 |
| Citation | Dmitriev RI, et al. (2007) Characterization of hampin/MSL1 as a node in the nuclear interactome. Biochem Biophys Res Commun 355(4):1051-7 |
| abstractText | Hampin, homolog of Drosophila MSL1, is a partner of histone acetyltransferase MYST1/MOF. Functions of these proteins remain poorly understood beyond their participation in chromatin remodeling complex MSL. In order to identify new proteins interacting with hampin, we screened a mouse cDNA library in yeast two-hybrid system with mouse hampin as bait and found five high-confidence interactors: MYST1, TPR proteins TTC4 and KIAA0103, NOP17 (homolog of a yeast nucleolar protein), and transcription factor GC BP. Subsequently, all these proteins were used as baits in library screenings and more new interactions were found: tumor suppressor RASSF1C and spliceosome component PRP3 for KIAA0103, ring finger RNF10 for RASSF1C, and RNA polymerase II regulator NELF-C for MYST1. The majority of the observed interactions was confirmed in vitro by pull-down of bacterially expressed proteins. Reconstruction of a fragment of mammalian interactome suggests that hampin may be linked to diverse regulatory processes in the nucleus. |
