The mobility of Bach2 nuclear foci is regulated by SUMO-1 modification.
The small ubiquitin-like modifier-1 (SUMO-1) modulates the functions of nuclear proteins by changing their structure and/or subnuclear localization. Several nuclear proteins form dynamic higher order nuclear structures, termed non-chromatin nuclear domains, which are involved in the regulation of nuclear function. However, the role that SUMO modification of the component proteins plays in the regulation of the activity and function of nuclear domains is unclear. Here we demonstrate that nuclear domains formed by Bach2, a transcription repressor, show restricted movement and undergo fusion events upon oxidative stress. Mutation of the SUMO-acceptor lysines in Bach2 alters the behavior of these nuclear foci and results in a decreased frequency of fusion events. We propose that SUMO modification is an important regulatory system for the mobility of the nuclear domains formed by Bach2.
Kono
Kazuteru
K
Department of Cellular Biology, Research Institute for Radiation Biology and Medicine, Hiroshima University, Kasumi 1-2-3, Minamiku, Hiroshima 734-8553, Japan.
Harano
Yumi
Y
Hoshino
Hideto
H
Kobayashi
Masao
M
Bazett-Jones
David P
DP
Muto
Akihiko
A
Igarashi
Kazuhiko
K
Tashiro
Satoshi
S
D050976:Basic-Leucine Zipper Transcription Factors / Q000032:analysis / Q000378:metabolism*; D002461:Cell Line, Transformed; D022003:Cell Nucleus Structures / Q000737:chemistry / Q000378:metabolism*; D004058:Diffusion; D036681:Fluorescence Recovery After Photobleaching; D006801:Humans; D018384:Oxidative Stress; D025842:SUMO-1 Protein / Q000378:metabolism*
C491123:BACH2 protein, human; D050976:Basic-Leucine Zipper Transcription Factors; D025842:SUMO-1 Protein