This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fang, J.
Right arrow Articles by Zhang, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fang, J.
Right arrow Articles by Zhang, Y.

 Previous Article

Molecular and Cellular Biology, July 2007, p. 5055-5065, Vol. 27, No. 13
0270-7306/07/$08.00+0     doi:10.1128/MCB.00127-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The Saccharomyces cerevisiae Histone Demethylase Jhd1 Fine-Tunes the Distribution of H3K36me2{triangledown}

Jia Fang,1,2 Gregory J. Hogan,3 Gaoyang Liang,1,2 Jason D. Lieb,3 and Yi Zhang1,2*

Howard Hughes Medical Institute,1 Department of Biochemistry and Biophysics, Lineberger Comprehensive Cancer Center,2 Department of Biology and the Carolina Center for Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 275993

Received 19 January 2007/ Returned for modification 26 February 2007/ Accepted 18 April 2007

Histone methylation plays important roles in the regulation of chromatin dynamics and transcription. Steady-state levels of histone lysine methylation are regulated by a balance between enzymes that catalyze either the addition or removal of methyl groups. Using an activity-based biochemical approach, we recently uncovered the JmjC domain as an evolutionarily conserved signature motif for histone demethylases. Furthermore, we demonstrated that Jhd1, a JmjC domain-containing protein in Saccharomyces cerevisiae, is an H3K36-specific demethylase. Here we report further characterization of Jhd1. Similar to its mammalian homolog, Jhd1-catalyzed histone demethylation requires iron and {alpha}-ketoglutarate as cofactors. Mutation and deletion studies indicate that the JmjC domain and adjacent sequences are critical for Jhd1 enzymatic activity, while the N-terminal PHD domain is dispensable. Overexpression of JHD1 results in a global reduction of H3K36 methylation in vivo. Finally, chromatin immunoprecipitation-coupled microarray studies reveal subtle changes in the distribution of H3K36me2 upon overexpression or deletion of JHD1. Our studies establish Jhd1 as a histone demethylase in budding yeast and suggest that Jhd1 functions to maintain the fidelity of histone methylation patterns along transcription units.

* Corresponding author. Mailing address: Lineberger Comprehensive Cancer Center, Campus Box 7295, University of North Carolina, Chapel Hill, NC 27599. Phone: (919) 843-8225. Fax: (919) 966-4330. E-mail: yi_zhang{at}med.unc.edu

{triangledown} Published ahead of print on 30 April 2007.

Molecular and Cellular Biology, July 2007, p. 5055-5065, Vol. 27, No. 13
0270-7306/07/$08.00+0     doi:10.1128/MCB.00127-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Ingvarsdottir, K., Edwards, C., Lee, M. G., Lee, J. S., Schultz, D. C., Shilatifard, A., Shiekhattar, R., Berger, S. L. (2007). Histone H3 K4 Demethylation during Activation and Attenuation of GAL1 Transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 27: 7856-7864 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»