Proliferating cell nuclear antigen is required for loading of the SMCX/KMD5C histone demethylase onto chromatin

<p>Abstract</p> <p>Background</p> <p>Histone methylation is regulated by a large number of histone methyltransferases and demethylases. The recently discovered SMCX/KMD5C demethylase has been shown to remove methyl residues from lysine 4 of histone H3 (H3K4), and consti...

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Main Authors: Liang Zhihui, Diamond Marc, Smith Johanna A, Schnell Matthias, Daniel René
Format: Article
Language:English
Published: BMC 2011-10-01
Series:Epigenetics & Chromatin
Online Access:http://www.epigeneticsandchromatin.com/content/4/1/18
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spelling doaj-24d17c79ada64341a5856fb1a90d656f2020-11-24T21:07:56ZengBMCEpigenetics & Chromatin1756-89352011-10-01411810.1186/1756-8935-4-18Proliferating cell nuclear antigen is required for loading of the SMCX/KMD5C histone demethylase onto chromatinLiang ZhihuiDiamond MarcSmith Johanna ASchnell MatthiasDaniel René<p>Abstract</p> <p>Background</p> <p>Histone methylation is regulated by a large number of histone methyltransferases and demethylases. The recently discovered SMCX/KMD5C demethylase has been shown to remove methyl residues from lysine 4 of histone H3 (H3K4), and constitutes an important component of the regulatory element-1-silencing transcription factor (REST) protein complex. However, little is known about the cellular mechanisms that control SMCX activity and intracellular trafficking.</p> <p>Results</p> <p>In this study, we found that small interfering RNA-mediated knockdown of proliferating cell nuclear antigen (PCNA) resulted in the reduction of the chromatin-bound SMCX fraction. We identified a PCNA-interaction protein motif (PIP box) in the SMCX protein. Using site-directed mutagenesis, we found that the amino acids of the SMCX PIP box are involved in the association of SMCX with PCNA and its interaction with chromatin.</p> <p>Conclusions</p> <p>Our data indicate that the intracellular trafficking of SMCX is controlled by its association with PCNA.</p> http://www.epigeneticsandchromatin.com/content/4/1/18
collection DOAJ
language English
format Article
sources DOAJ
author Liang Zhihui
Diamond Marc
Smith Johanna A
Schnell Matthias
Daniel René
spellingShingle Liang Zhihui
Diamond Marc
Smith Johanna A
Schnell Matthias
Daniel René
Proliferating cell nuclear antigen is required for loading of the SMCX/KMD5C histone demethylase onto chromatin
Epigenetics & Chromatin
author_facet Liang Zhihui
Diamond Marc
Smith Johanna A
Schnell Matthias
Daniel René
author_sort Liang Zhihui
title Proliferating cell nuclear antigen is required for loading of the SMCX/KMD5C histone demethylase onto chromatin
title_short Proliferating cell nuclear antigen is required for loading of the SMCX/KMD5C histone demethylase onto chromatin
title_full Proliferating cell nuclear antigen is required for loading of the SMCX/KMD5C histone demethylase onto chromatin
title_fullStr Proliferating cell nuclear antigen is required for loading of the SMCX/KMD5C histone demethylase onto chromatin
title_full_unstemmed Proliferating cell nuclear antigen is required for loading of the SMCX/KMD5C histone demethylase onto chromatin
title_sort proliferating cell nuclear antigen is required for loading of the smcx/kmd5c histone demethylase onto chromatin
publisher BMC
series Epigenetics & Chromatin
issn 1756-8935
publishDate 2011-10-01
description <p>Abstract</p> <p>Background</p> <p>Histone methylation is regulated by a large number of histone methyltransferases and demethylases. The recently discovered SMCX/KMD5C demethylase has been shown to remove methyl residues from lysine 4 of histone H3 (H3K4), and constitutes an important component of the regulatory element-1-silencing transcription factor (REST) protein complex. However, little is known about the cellular mechanisms that control SMCX activity and intracellular trafficking.</p> <p>Results</p> <p>In this study, we found that small interfering RNA-mediated knockdown of proliferating cell nuclear antigen (PCNA) resulted in the reduction of the chromatin-bound SMCX fraction. We identified a PCNA-interaction protein motif (PIP box) in the SMCX protein. Using site-directed mutagenesis, we found that the amino acids of the SMCX PIP box are involved in the association of SMCX with PCNA and its interaction with chromatin.</p> <p>Conclusions</p> <p>Our data indicate that the intracellular trafficking of SMCX is controlled by its association with PCNA.</p>
url http://www.epigeneticsandchromatin.com/content/4/1/18
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AT smithjohannaa proliferatingcellnuclearantigenisrequiredforloadingofthesmcxkmd5chistonedemethylaseontochromatin
AT schnellmatthias proliferatingcellnuclearantigenisrequiredforloadingofthesmcxkmd5chistonedemethylaseontochromatin
AT danielrene proliferatingcellnuclearantigenisrequiredforloadingofthesmcxkmd5chistonedemethylaseontochromatin
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