title: The jmjN and jmjC domains of the yeast zinc finger protein Gis1 interact with 19 proteins involved in transcription, sumoylation and DNA repair.
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.
authors.affiliation: Department of Plant Biology and Forest Genetics, Swedish University of Agricultural Sciences, P.O. Box 7080, 75007, Uppsala, Sweden.
authors.forename: Susanna
authors.initials: S
authors.lastname: Tronnersjö
authors.forename: Christine
authors.initials: C
authors.lastname: Hanefalk
authors.forename: Darius
authors.initials: D
authors.lastname: Balciunas
authors.forename: Guo-Zhen
authors.initials: GZ
authors.lastname: Hu
authors.forename: Niklas
authors.initials: N
authors.lastname: Nordberg
authors.forename: Eva
authors.initials: E
authors.lastname: Murén
authors.forename: Hans
authors.initials: H
authors.lastname: Ronne
mesh_terms: D005090:Exodeoxyribonucleases; D006801:Humans; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding / Q000235:genetics; D011499:Protein Processing, Post-Translational / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000235:genetics; D053484:RecQ Helicases / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D025841:Small Ubiquitin-Related Modifier Proteins / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic / Q000235:genetics; D020798:Two-Hybrid System Techniques; D000071657:Werner Syndrome Helicase
chemical_list: C495981:Esc1 protein, S cerevisiae; D018832:Molecular Chaperones; D009687:Nuclear Proteins; C061573:SIR4 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae; C436836:Siz2 protein, S cerevisiae; D025841:Small Ubiquitin-Related Modifier Proteins; C112806:prefoldin; D005090:Exodeoxyribonucleases; C090472:SGS1 protein, S cerevisiae; D053484:RecQ Helicases; C098785:WRN protein, human; D000071657:Werner Syndrome Helicase