Campus Units
Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of
Document Type
Article
Publication Version
Published Version
Publication Date
7-5-2013
Journal or Book Title
Journal of Biological Chemistry
Volume
288
Issue
27
First Page
19441
Last Page
19449
DOI
10.1074/jbc.M113.464271
Abstract
The JIL-1 kinase localizes to Drosophila polytene chromosome interbands and phosphorylates histone H3 at interphase, counteracting histone H3 lysine 9 dimethylation and gene silencing. JIL-1 can be divided into four main domains, including an NH2-terminal domain, two separate kinase domains, and a COOH-terminal domain. In this study, we characterize the domain requirements of the JIL-1 kinase for histone H3 serine 10 (H3S10) phosphorylation and chromatin remodeling in vivo. We show that a JIL-1 construct without the NH2-terminal domain is without H3S10 phosphorylation activity despite the fact that it localizes properly to polytene interband regions and that it contains both kinase domains. JIL-1 is a double kinase, and we demonstrate that both kinase domains of JIL-1 are required to be catalytically active for H3S10 phosphorylation to occur. Furthermore, we provide evidence that JIL-1 is phosphorylated at serine 424 and that this phosphorylation is necessary for JIL-1 H3S10 phosphorylation activity. Thus, these data are compatible with a model where the NH2-terminal domain of JIL-1 is required for chromatin complex interactions that position the kinase domain(s) for catalytic activity in the context of the state of higher order nucleosome packaging and chromatin structure and where catalytic H3S10 phosphorylation activity mediated by the first kinase domain is dependent on autophosphorylation of serine 424 by the second kinase domain. Furthermore, using a lacO repeat tethering system to target mutated JIL-1 constructs with or without catalytic activity, we show that the epigenetic H3S10 phosphorylation mark itself functions as a causative regulator of chromatin structure independently of any structural contributions from the JIL-1 protein.
Copyright Owner
The American Society for Biochemistry and Molecular Biology, Inc.
Copyright Date
2013
Language
en
File Format
application/pdf
Recommended Citation
Li, Yeran; Cai, Weili; Wang, Chao; Yao, Changfu; Bao, Xiaomin; Deng, Huai; Girton, Jack; Johansen, Jorgen; and Johansen, Kristen M., "Domain Requirements of the JIL-1 Tandem Kinase for Histone H3 Serine 10 Phosphorylation and Chromatin Remodeling in Vivo" (2013). Biochemistry, Biophysics and Molecular Biology Publications. 246.
https://lib.dr.iastate.edu/bbmb_ag_pubs/246
Included in
Biochemistry Commons, Biophysics Commons, Molecular Biology Commons, Structural Biology Commons
Comments
This research was originally published in the Journal of Biological Chemistry. Li, Yeran, Weili Cai, Chao Wang, Changfu Yao, Xiaomin Bao, Huai Deng, Jack Girton, Jørgen Johansen, and Kristen M. Johansen. "Domain requirements of the JIL-1 tandem kinase for histone H3 Serine 10 phosphorylation and chromatin remodeling in vivo." Journal of Biological Chemistry 288, no. 27 (2013): 19441-19449. © the American Society for Biochemistry and Molecular Biology. doi: 10.1074/jbc.M113.464271.