TY - JOUR
T1 - Middle-down and top-down mass spectrometric analysis of co-occurring histone modifications
AU - Molden, Rosalynn C.
AU - Garcia, Benjamin A.
N1 - Publisher Copyright:
© 2014 by John Wiley & Sons, Inc.
PY - 2014
Y1 - 2014
N2 - Histones are chromatin proteins that are highly modified with many different types of post-translational modifications. These modifications act in concert to regulate a number of chromatin-related processes. However, identification and quantification of co-occurring histone post-translational modifications is challenging because there are many potential combinations of modifications and because the commonly used strategy of fragmenting proteins using trypsin or an alternative protease prior to LC-MS/MS analysis results in the loss of connectivity between modifications on different peptides. In this unit, mass spectrometric methods to analyze combinatorial histone modifications on histone tails (middle-down mass spectrometry) and on intact histones (top-down mass spectrometry) are described.
AB - Histones are chromatin proteins that are highly modified with many different types of post-translational modifications. These modifications act in concert to regulate a number of chromatin-related processes. However, identification and quantification of co-occurring histone post-translational modifications is challenging because there are many potential combinations of modifications and because the commonly used strategy of fragmenting proteins using trypsin or an alternative protease prior to LC-MS/MS analysis results in the loss of connectivity between modifications on different peptides. In this unit, mass spectrometric methods to analyze combinatorial histone modifications on histone tails (middle-down mass spectrometry) and on intact histones (top-down mass spectrometry) are described.
KW - Histone modifications
KW - Middle-down mass spectrometry
KW - Post-translational modifications
KW - Top-down mass spectrometry
UR - http://www.scopus.com/inward/record.url?scp=84949196237&partnerID=8YFLogxK
U2 - 10.1002/0471140864.ps2307s77
DO - 10.1002/0471140864.ps2307s77
M3 - Article
C2 - 25081742
AN - SCOPUS:84949196237
SN - 1934-3655
VL - 2014
SP - 23.7.1-23.7.28
JO - Current protocols in protein science / editorial board, John E. Coligan ... [et al.]
JF - Current protocols in protein science / editorial board, John E. Coligan ... [et al.]
ER -