Original Paper

Molecular Genetics and Genomics

, Volume 277, Issue 1, pp 57-70

First online:

The jmjN and jmjC domains of the yeast zinc finger protein Gis1 interact with 19 proteins involved in transcription, sumoylation and DNA repair

  • Susanna TronnersjöAffiliated withDepartment of Plant Biology and Forest Genetics, Swedish University of Agricultural SciencesDepartment of Medical Biochemistry and Microbiology, Uppsala University
  • , Christine HanefalkAffiliated withDepartment of Plant Biology and Forest Genetics, Swedish University of Agricultural Sciences
  • , Darius BalciunasAffiliated withDepartment of Plant Biology and Forest Genetics, Swedish University of Agricultural SciencesDepartment of Medical Biochemistry and Microbiology, Uppsala UniversityDepartment of Genetics, Cell Biology and Development, University of Minnesota
  • , Guo-Zhen HuAffiliated withDepartment of Plant Biology and Forest Genetics, Swedish University of Agricultural SciencesDepartment of Medical Biochemistry and Microbiology, Uppsala University
  • , Niklas NordbergAffiliated withDepartment of Medical Biochemistry and Microbiology, Uppsala University
  • , Eva MurénAffiliated withDepartment of Plant Biology and Forest Genetics, Swedish University of Agricultural SciencesDepartment of Medical Biochemistry and Microbiology, Uppsala University
  • , Hans RonneAffiliated withDepartment of Plant Biology and Forest Genetics, Swedish University of Agricultural SciencesDepartment of Medical Biochemistry and Microbiology, Uppsala University Email author 

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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.

Keywords

Bud27 Gis1 jmjC Sgs1 Sumoylation