Molecular Genetics and Genomics

, Volume 277, Issue 1, pp 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

Authors

  • Susanna Tronnersjö
    • Department of Plant Biology and Forest GeneticsSwedish University of Agricultural Sciences
    • Department of Medical Biochemistry and MicrobiologyUppsala University
  • Christine Hanefalk
    • Department of Plant Biology and Forest GeneticsSwedish University of Agricultural Sciences
  • Darius Balciunas
    • Department of Plant Biology and Forest GeneticsSwedish University of Agricultural Sciences
    • Department of Medical Biochemistry and MicrobiologyUppsala University
    • Department of Genetics, Cell Biology and DevelopmentUniversity of Minnesota
  • Guo-Zhen Hu
    • Department of Plant Biology and Forest GeneticsSwedish University of Agricultural Sciences
    • Department of Medical Biochemistry and MicrobiologyUppsala University
  • Niklas Nordberg
    • Department of Medical Biochemistry and MicrobiologyUppsala University
  • Eva Murén
    • Department of Plant Biology and Forest GeneticsSwedish University of Agricultural Sciences
    • Department of Medical Biochemistry and MicrobiologyUppsala University
    • Department of Plant Biology and Forest GeneticsSwedish University of Agricultural Sciences
    • Department of Medical Biochemistry and MicrobiologyUppsala University
Original Paper

DOI: 10.1007/s00438-006-0171-3

Cite this article as:
Tronnersjö, S., Hanefalk, C., Balciunas, D. et al. Mol Genet Genomics (2007) 277: 57. doi:10.1007/s00438-006-0171-3

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

Bud27Gis1jmjCSgs1Sumoylation

Copyright information

© Springer-Verlag 2006