Precision mapping of coexisting modifications in histone H3 tails from embryonic stem cells by ETD-MS/MS
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Precision mapping of coexisting modifications in histone H3 tails from embryonic stem cells by ETD-MS/MS. / Jung, Hye Ryung; Sidoli, Simone; Haldbo, Simon; Sprenger, Richard; Schwämmle, Veit; Pasini, Diego; Helin, Kristian; Jensen, Ole.
In: Analytical Chemistry, Vol. 85, No. 17, 03.09.2013, p. 8232-9.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Precision mapping of coexisting modifications in histone H3 tails from embryonic stem cells by ETD-MS/MS
AU - Jung, Hye Ryung
AU - Sidoli, Simone
AU - Haldbo, Simon
AU - Sprenger, Richard
AU - Schwämmle, Veit
AU - Pasini, Diego
AU - Helin, Kristian
AU - Jensen, Ole
PY - 2013/9/3
Y1 - 2013/9/3
N2 - Post-translational modifications (PTMs) of histones play a major role in regulating chromatin dynamics and influence processes such as transcription and DNA replication. Here, we report 114 distinct combinations of coexisting PTMs of histone H3 obtained from mouse embryonic stem (ES) cells. Histone H3 N-terminal tail peptides (amino acids 1-50, 5-6 kDa) were separated by optimized weak cation exchange/hydrophilic interaction liquid chromatography (WCX/HILIC) and sequenced online by electron transfer dissociation (ETD) tandem mass spectrometry (MS/MS). High mass accuracy and near complete sequence coverage allowed unambiguous mapping of the major histone marks and discrimination between isobaric and nearly isobaric PTMs such as trimethylation and acetylation. Hierarchical data analysis identified H3K27me2-H3K36me2 as the most frequently observed PTMs in H3. Modifications at H3 residues K27 and K36 often coexist with the abundant mark K23ac, and we identified two frequently occurring quadruplet marks 'K9me1K23acK27me2K36me2' and 'K9me3K23acK27me2K36me', which might indicate a role in crosstalk. Co-occurrence frequency analysis revealed also an interplay between methylations of K9, K27, and K36, suggesting interdependence between histone methylation marks. We hypothesize that the most abundant coexisting PTMs may provide a signature for the permissive state of mouse ES cells.
AB - Post-translational modifications (PTMs) of histones play a major role in regulating chromatin dynamics and influence processes such as transcription and DNA replication. Here, we report 114 distinct combinations of coexisting PTMs of histone H3 obtained from mouse embryonic stem (ES) cells. Histone H3 N-terminal tail peptides (amino acids 1-50, 5-6 kDa) were separated by optimized weak cation exchange/hydrophilic interaction liquid chromatography (WCX/HILIC) and sequenced online by electron transfer dissociation (ETD) tandem mass spectrometry (MS/MS). High mass accuracy and near complete sequence coverage allowed unambiguous mapping of the major histone marks and discrimination between isobaric and nearly isobaric PTMs such as trimethylation and acetylation. Hierarchical data analysis identified H3K27me2-H3K36me2 as the most frequently observed PTMs in H3. Modifications at H3 residues K27 and K36 often coexist with the abundant mark K23ac, and we identified two frequently occurring quadruplet marks 'K9me1K23acK27me2K36me2' and 'K9me3K23acK27me2K36me', which might indicate a role in crosstalk. Co-occurrence frequency analysis revealed also an interplay between methylations of K9, K27, and K36, suggesting interdependence between histone methylation marks. We hypothesize that the most abundant coexisting PTMs may provide a signature for the permissive state of mouse ES cells.
U2 - 10.1021/ac401299w
DO - 10.1021/ac401299w
M3 - Journal article
C2 - 23889513
VL - 85
SP - 8232
EP - 8239
JO - Industrial And Engineering Chemistry Analytical Edition
JF - Industrial And Engineering Chemistry Analytical Edition
SN - 0003-2700
IS - 17
ER -
ID: 94394259