The Jumonji C Domain-Containing Protein JMJ30 Regulates Period Length in the Arabidopsis Circadian Clock1[W][OA]
Histone methylation plays an essential role in regulating chromatin structure and gene expression. Jumonji C (JmjC) domain-containing proteins are generally known as histone demethylases. Circadian clocks regulate a large number of biological processes, and recent studies suggest that chromatin remo...
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Published in | Plant physiology (Bethesda) Vol. 155; no. 2; pp. 906 - 915 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
American Society of Plant Biologists
07.12.2010
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Subjects | |
Online Access | Get full text |
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Summary: | Histone methylation plays an essential role in regulating chromatin structure and gene expression. Jumonji C (JmjC) domain-containing proteins are generally known as histone demethylases. Circadian clocks regulate a large number of biological processes, and recent studies suggest that chromatin remodeling has evolved as an important mechanism for regulating both plant and mammalian circadian systems. Here, we analyzed a subgroup of JmjC domain-containing proteins and identified Arabidopsis (
Arabidopsis thaliana
) JMJ30 as a novel clock component involved in controlling the circadian period. Analysis of loss- and gain-of-function mutants of
JMJ30
indicates that this evening-expressed gene is a genetic regulator of period length in the Arabidopsis circadian clock. Furthermore, two key components of the central oscillator of plants, transcription factors CIRCADIAN CLOCK ASSOCIATED1 and LATE ELONGATED HYPOCOTYL, bind directly to the
JMJ30
promoter to repress its expression, suggesting that JMJ30 regulates the pace of the circadian clock in close association with the central oscillator. JMJ30 represents, to our knowledge, the first JmjC domain-containing protein involved in circadian function, and we envision that this provides a possible molecular connection between chromatin remodeling and the circadian clock. |
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Bibliography: | The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Elaine M. Tobin (etobin@ucla.edu). This work was supported by the National Institutes of Health (grant no. GM23167 to E.M.T.). The online version of this article contains Web-only data. www.plantphysiol.org/cgi/doi/10.1104/pp.110.167015 Present address: 1571 N. Salisbury St., Porterville, CA 93257. Open Access articles can be viewed online without a subscription. Present address: 432 E. Poplar Ave., Vallejo, CA 94592. |
ISSN: | 0032-0889 1532-2548 |
DOI: | 10.1104/pp.110.167015 |