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	Mol. Genet. Genomics Jan (2007); 277(1):57-70
The jmjN and jmjC domains of the yeast zinc finger protein Gis1 interact with 19 proteins involved in transcription, sumoylation and DNA repair-
Tronnersjo S, Hanefalk C, Balciunas D, Hu GZ, Nordberg N, Muren E, Ronne H
Department of Plant Biology and Forest Genetics, Swedish University of Agricultural Sciences, P-O- Box 7080, 75007, Uppsala, Sweden-
Abstract: The jumonji domain is a highly conserved bipartite domain made up of two subdomains, jmjN and jmjC, which is found in many eukaryotic transcription factors- The jmjC domain was recently shown to possess the histone demethylase activity- Here we show that the jmjN and jmjC domains of the yeast zinc finger protein Gis1 interact in a two-hybrid system with 19 yeast proteins that include the RecQ helicase Sgs1, the silencing factors Esc1 and Sir4, the URI-type prefoldin Bud27 and the PIAS type SUMO ligase Nfi1-Siz2- Extensive interaction cross dependencies further suggest that the proteins form a larger complex- Consistent with this, 16 of the proteins also interact with a Bud27 two-hybrid bait, and three of them co-precipitate with TAP-tagged Gis1- The Gis1 jumonji domain can repress transcription when recruited to a promoter as a lexA fusion- This effect is dependent on both the jmjN and jmjC subdomains, as were all 19 two-hybrid interactions, indicating that the two subdomains form a single functional unit- The human Sgs1 homolog WRN also interacts with the Gis1 jumonji domain- Finally, we note that several jumonji domain interactors are related to proteins that are found in mammalian PML nuclear bodies-
[PUBMED: 17043893]

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