TY - JOUR
T1 - Mass spectrometry analysis of Arabidopsis histone H3 reveals distinct combinations of post-translational modifications
AU - Johnson, Lianna
AU - Mollah, Sahana
AU - Garcia, Benjamin A.
AU - Muratore, Tara L.
AU - Shabanowitz, Jeffrey
AU - Hunt, Donald F.
AU - Jacobsen, Steven E.
N1 - Funding Information:
We thank Simon Chan and Anders Lindroth for critically reading this manuscript. This work was supported in part by Beckman Young Investigator Award (S.E.J.) and NIH grant GM37537 (D.F.H.).
PY - 2004
Y1 - 2004
N2 - Chromatin is regulated at many different levels, from higher-order packing to individual nucleosome placement. Recent studies have shown that individual histone modifications, and combinations thereof, play a key role in modulating chromatin structure and gene activity. Reported here is an analysis of Arabidopsis histone H3 modifications by nanoflow-HPLC coupled to electrospray ionization on a hybrid linear ion trap-Fourier transform mass spectrometer (LTQ/FTMS). We find that the sites of acetylation and methylation, in general, correlate well with other plants and animals. Two well-studied modifications, dimethylation of Lys-9 (correlated with silencing) and acetylation of Lys-14 (correlated with active chromatin) while abundant by themselves were rarely found on the same histone H3 tail. In contrast, dimethylation at Lys-27 and monomethylation at Lys-36 were commonly found together. Interestingly, acetylation at Lys-9 was found only in a low percentage of histories while acetylation of Lys-14 was very abundant. The two histone H3 variants, H3.1 and H3.2, also differ in the abundance of silencing and activating marks confirming other studies showing that the replication-independent histone H3 is enriched in active chromatin.
AB - Chromatin is regulated at many different levels, from higher-order packing to individual nucleosome placement. Recent studies have shown that individual histone modifications, and combinations thereof, play a key role in modulating chromatin structure and gene activity. Reported here is an analysis of Arabidopsis histone H3 modifications by nanoflow-HPLC coupled to electrospray ionization on a hybrid linear ion trap-Fourier transform mass spectrometer (LTQ/FTMS). We find that the sites of acetylation and methylation, in general, correlate well with other plants and animals. Two well-studied modifications, dimethylation of Lys-9 (correlated with silencing) and acetylation of Lys-14 (correlated with active chromatin) while abundant by themselves were rarely found on the same histone H3 tail. In contrast, dimethylation at Lys-27 and monomethylation at Lys-36 were commonly found together. Interestingly, acetylation at Lys-9 was found only in a low percentage of histories while acetylation of Lys-14 was very abundant. The two histone H3 variants, H3.1 and H3.2, also differ in the abundance of silencing and activating marks confirming other studies showing that the replication-independent histone H3 is enriched in active chromatin.
UR - http://www.scopus.com/inward/record.url?scp=13544271154&partnerID=8YFLogxK
U2 - 10.1093/nar/gkh992
DO - 10.1093/nar/gkh992
M3 - Article
C2 - 15598823
AN - SCOPUS:13544271154
SN - 0305-1048
VL - 32
SP - 6511
EP - 6518
JO - Nucleic acids research
JF - Nucleic acids research
IS - 22
ER -