Identification of lysine 37 of histone H2B as a novel site of methylation.

Recent technological advancements have allowed for highly-sophisticated mass spectrometry-based studies of the histone code, which predicts that combinations of post-translational modifications (PTMs) on histone proteins result in defined biological outcomes mediated by effector proteins that recogn...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Kathryn E Gardner, Li Zhou, Michael A Parra, Xian Chen, Brian D Strahl
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ff3b6eb192df48c5be6fe480e546c378
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:ff3b6eb192df48c5be6fe480e546c378
record_format	dspace
spelling	oai:doaj.org-article:ff3b6eb192df48c5be6fe480e546c3782021-11-18T07:00:31ZIdentification of lysine 37 of histone H2B as a novel site of methylation.1932-620310.1371/journal.pone.0016244https://doaj.org/article/ff3b6eb192df48c5be6fe480e546c3782011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21249157/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Recent technological advancements have allowed for highly-sophisticated mass spectrometry-based studies of the histone code, which predicts that combinations of post-translational modifications (PTMs) on histone proteins result in defined biological outcomes mediated by effector proteins that recognize such marks. While significant progress has been made in the identification and characterization of histone PTMs, a full appreciation of the complexity of the histone code will require a complete understanding of all the modifications that putatively contribute to it. Here, using the top-down mass spectrometry approach for identifying PTMs on full-length histones, we report that lysine 37 of histone H2B is dimethylated in the budding yeast Saccharomyces cerevisiae. By generating a modification-specific antibody and yeast strains that harbor mutations in the putative site of methylation, we provide evidence that this mark exist in vivo. Importantly, we show that this lysine residue is highly conserved through evolution, and provide evidence that this methylation event also occurs in higher eukaryotes. By identifying a novel site of histone methylation, this study adds to our overall understanding of the complex number of histone modifications that contribute to chromatin function.Kathryn E GardnerLi ZhouMichael A ParraXian ChenBrian D StrahlPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 1, p e16244 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kathryn E Gardner Li Zhou Michael A Parra Xian Chen Brian D Strahl Identification of lysine 37 of histone H2B as a novel site of methylation.
description	Recent technological advancements have allowed for highly-sophisticated mass spectrometry-based studies of the histone code, which predicts that combinations of post-translational modifications (PTMs) on histone proteins result in defined biological outcomes mediated by effector proteins that recognize such marks. While significant progress has been made in the identification and characterization of histone PTMs, a full appreciation of the complexity of the histone code will require a complete understanding of all the modifications that putatively contribute to it. Here, using the top-down mass spectrometry approach for identifying PTMs on full-length histones, we report that lysine 37 of histone H2B is dimethylated in the budding yeast Saccharomyces cerevisiae. By generating a modification-specific antibody and yeast strains that harbor mutations in the putative site of methylation, we provide evidence that this mark exist in vivo. Importantly, we show that this lysine residue is highly conserved through evolution, and provide evidence that this methylation event also occurs in higher eukaryotes. By identifying a novel site of histone methylation, this study adds to our overall understanding of the complex number of histone modifications that contribute to chromatin function.
format	article
author	Kathryn E Gardner Li Zhou Michael A Parra Xian Chen Brian D Strahl
author_facet	Kathryn E Gardner Li Zhou Michael A Parra Xian Chen Brian D Strahl
author_sort	Kathryn E Gardner
title	Identification of lysine 37 of histone H2B as a novel site of methylation.
title_short	Identification of lysine 37 of histone H2B as a novel site of methylation.
title_full	Identification of lysine 37 of histone H2B as a novel site of methylation.
title_fullStr	Identification of lysine 37 of histone H2B as a novel site of methylation.
title_full_unstemmed	Identification of lysine 37 of histone H2B as a novel site of methylation.
title_sort	identification of lysine 37 of histone h2b as a novel site of methylation.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/ff3b6eb192df48c5be6fe480e546c378
work_keys_str_mv	AT kathrynegardner identificationoflysine37ofhistoneh2basanovelsiteofmethylation AT lizhou identificationoflysine37ofhistoneh2basanovelsiteofmethylation AT michaelaparra identificationoflysine37ofhistoneh2basanovelsiteofmethylation AT xianchen identificationoflysine37ofhistoneh2basanovelsiteofmethylation AT briandstrahl identificationoflysine37ofhistoneh2basanovelsiteofmethylation
_version_	1718424081294950400

Identification of lysine 37 of histone H2B as a novel site of methylation.

Ejemplares similares