TY - JOUR
T1 - Epiproteomics
T2 - Quantitative analysis of histone marks and codes by mass spectrometry
AU - Zheng, Yupeng
AU - Huang, Xiaoxiao
AU - Kelleher, Neil L.
N1 - Funding Information:
This review was written with partial support from the National Resource for Translational and Developmental Proteomics under Grant P41 GM108569 from the National Institute of General Medical Sciences , National Institutes of Health .
Publisher Copyright:
© 2016.
PY - 2016/8/1
Y1 - 2016/8/1
N2 - Histones are a group of proteins with a high number of post-translational modifications, including methylation, acetylation, phosphorylation, and monoubiquitination, which play critical roles in every chromatin-templated activity. The quantitative analysis of these modifications using mass spectrometry (MS) has seen significant improvements over the last decade. It is now possible to perform large-scale surveys of dozens of histone marks and hundreds of their combinations on global chromatin. Here, we review the development of three MS strategies for analyzing histone modifications that have come to be known as Bottom Up, Middle Down, and Top Down. We also discuss challenges and innovative solutions for characterizing and quantifying complicated isobaric species arising from multiple modifications on the same histone molecule.
AB - Histones are a group of proteins with a high number of post-translational modifications, including methylation, acetylation, phosphorylation, and monoubiquitination, which play critical roles in every chromatin-templated activity. The quantitative analysis of these modifications using mass spectrometry (MS) has seen significant improvements over the last decade. It is now possible to perform large-scale surveys of dozens of histone marks and hundreds of their combinations on global chromatin. Here, we review the development of three MS strategies for analyzing histone modifications that have come to be known as Bottom Up, Middle Down, and Top Down. We also discuss challenges and innovative solutions for characterizing and quantifying complicated isobaric species arising from multiple modifications on the same histone molecule.
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U2 - 10.1016/j.cbpa.2016.06.007
DO - 10.1016/j.cbpa.2016.06.007
M3 - Review article
C2 - 27371874
AN - SCOPUS:84976447995
SN - 1367-5931
VL - 33
SP - 142
EP - 150
JO - Current Opinion in Chemical Biology
JF - Current Opinion in Chemical Biology
ER -