The human proteins MBD5 and MBD6 associate with heterochromatin but they do not bind methylated DNA.

<h4>Background</h4>MBD5 and MBD6 are two uncharacterized mammalian proteins that contain a putative Methyl-Binding Domain (MBD). In the proteins MBD1, MBD2, MBD4, and MeCP2, this domain allows the specific recognition of DNA containing methylated cytosine; as a consequence, the proteins...

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Autores principales:	Sophie Laget, Michael Joulie, Florent Le Masson, Nobuhiro Sasai, Elisabeth Christians, Sriharsa Pradhan, Richard J Roberts, Pierre-Antoine Defossez
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/23e7c5a57b244ae4b24a4b6fb68b9666
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spelling	oai:doaj.org-article:23e7c5a57b244ae4b24a4b6fb68b96662021-11-18T06:36:22ZThe human proteins MBD5 and MBD6 associate with heterochromatin but they do not bind methylated DNA.1932-620310.1371/journal.pone.0011982https://doaj.org/article/23e7c5a57b244ae4b24a4b6fb68b96662010-08-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20700456/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>MBD5 and MBD6 are two uncharacterized mammalian proteins that contain a putative Methyl-Binding Domain (MBD). In the proteins MBD1, MBD2, MBD4, and MeCP2, this domain allows the specific recognition of DNA containing methylated cytosine; as a consequence, the proteins serve as interpreters of DNA methylation, an essential epigenetic mark. It is unknown whether MBD5 or MBD6 also bind methylated DNA; this question has interest for basic research, but also practical consequences for human health, as MBD5 deletions are the likely cause of certain cases of mental retardation.<h4>Principal findings</h4>Here we report the first functional characterization of MBD5 and MBD6. We have observed that the proteins colocalize with heterochromatin in cultured cells, and that this localization requires the integrity of their MBD. However, heterochromatic localization is maintained in cells with severely decreased levels of DNA methylation. In vitro, neither MBD5 nor MBD6 binds any of the methylated sequences DNA that were tested.<h4>Conclusions</h4>Our data suggest that MBD5 and MBD6 are unlikely to be methyl-binding proteins, yet they may contribute to the formation or function of heterochromatin. One isoform of MBD5 is highly expressed in oocytes, which suggests a possible role in epigenetic reprogramming after fertilization.Sophie LagetMichael JoulieFlorent Le MassonNobuhiro SasaiElisabeth ChristiansSriharsa PradhanRichard J RobertsPierre-Antoine DefossezPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 8, p e11982 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sophie Laget Michael Joulie Florent Le Masson Nobuhiro Sasai Elisabeth Christians Sriharsa Pradhan Richard J Roberts Pierre-Antoine Defossez The human proteins MBD5 and MBD6 associate with heterochromatin but they do not bind methylated DNA.
description	<h4>Background</h4>MBD5 and MBD6 are two uncharacterized mammalian proteins that contain a putative Methyl-Binding Domain (MBD). In the proteins MBD1, MBD2, MBD4, and MeCP2, this domain allows the specific recognition of DNA containing methylated cytosine; as a consequence, the proteins serve as interpreters of DNA methylation, an essential epigenetic mark. It is unknown whether MBD5 or MBD6 also bind methylated DNA; this question has interest for basic research, but also practical consequences for human health, as MBD5 deletions are the likely cause of certain cases of mental retardation.<h4>Principal findings</h4>Here we report the first functional characterization of MBD5 and MBD6. We have observed that the proteins colocalize with heterochromatin in cultured cells, and that this localization requires the integrity of their MBD. However, heterochromatic localization is maintained in cells with severely decreased levels of DNA methylation. In vitro, neither MBD5 nor MBD6 binds any of the methylated sequences DNA that were tested.<h4>Conclusions</h4>Our data suggest that MBD5 and MBD6 are unlikely to be methyl-binding proteins, yet they may contribute to the formation or function of heterochromatin. One isoform of MBD5 is highly expressed in oocytes, which suggests a possible role in epigenetic reprogramming after fertilization.
format	article
author	Sophie Laget Michael Joulie Florent Le Masson Nobuhiro Sasai Elisabeth Christians Sriharsa Pradhan Richard J Roberts Pierre-Antoine Defossez
author_facet	Sophie Laget Michael Joulie Florent Le Masson Nobuhiro Sasai Elisabeth Christians Sriharsa Pradhan Richard J Roberts Pierre-Antoine Defossez
author_sort	Sophie Laget
title	The human proteins MBD5 and MBD6 associate with heterochromatin but they do not bind methylated DNA.
title_short	The human proteins MBD5 and MBD6 associate with heterochromatin but they do not bind methylated DNA.
title_full	The human proteins MBD5 and MBD6 associate with heterochromatin but they do not bind methylated DNA.
title_fullStr	The human proteins MBD5 and MBD6 associate with heterochromatin but they do not bind methylated DNA.
title_full_unstemmed	The human proteins MBD5 and MBD6 associate with heterochromatin but they do not bind methylated DNA.
title_sort	human proteins mbd5 and mbd6 associate with heterochromatin but they do not bind methylated dna.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/23e7c5a57b244ae4b24a4b6fb68b9666
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The human proteins MBD5 and MBD6 associate with heterochromatin but they do not bind methylated DNA.

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