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...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2011-01, Vol.6 (1), p.e16244-e16244
Main Authors: Gardner, Kathryn E, Zhou, Li, Parra, Michael A, Chen, Xian, Strahl, Brian D
Format: Article
Language:English
Subjects:
Antibodies
Baking yeast
Biochemistry
Biological effects
Biology
Biophysics
Cancer
Chromatin
Complexity
Deoxyribonucleic acid
DNA
DNA binding proteins
DNA methylation
Eukaryotes
Evolution
Genetic aspects
Histone Code
Histone H2B
Histones
Histones - metabolism
Lysine
Lysine - metabolism
Mass spectrometry
Mass Spectrometry - methods
Mass spectroscopy
Medicine
Methylation
Mutation
Post-translation
Protein Processing, Post-Translational
Proteins
Recruitment
Saccharomyces cerevisiae
Saccharomyces cerevisiae - genetics
Spectroscopy
Tetrahymena
Yeast
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0016244