TY - JOUR
T1 - Organismal differences in post-translational modifications in histones H3 and H4
AU - Garcia, Benjamin A.
AU - Hake, Sandra B.
AU - Diaz, Robert L.
AU - Kauer, Monika
AU - Morris, Stephanie A.
AU - Recht, Judith
AU - Shabanowitz, Jeffrey
AU - Mishra, Nilamadhab
AU - Strahl, Brian D.
AU - Allis, C. David
AU - Hunt, Donald F.
PY - 2007/3/2
Y1 - 2007/3/2
N2 - Post-translational modifications (PTMs) of histones play an important role inmanycellular processes, notably gene regulation. Using a combination of mass spectrometric and immunobiochemical approaches, we show that the PTM profile of histone H3 differs significantly among the various model organisms examined. Unicellular eukaryotes, such as Saccharomyces cerevisiae (yeast) and Tetrahymena thermophila (Tet), for example, contain more activation than silencing marks as compared with mammalian cells (mouse and human), which are generally enriched in PTMs more often associated with gene silencing. Close examination reveals that many of the better-known modified lysines (Lys) can be either methylated or acetylated and that the overall modification patterns become more complex from unicellular eukaryotes to mammals. Additionally, novel species-specific H3 PTMs from wild-type asynchronously grown cells are also detected by mass spectrometry. Our results suggest that some PTMs are more conserved than previously thought, including H3K9me1 and H4K20me2 in yeast and H3K27me1, -me2, and -me3 in Tet. On histone H4, methylation at Lys-20 showed a similar pattern as H3 methylation at Lys-9, with mammals containing more methylation than the unicellular organisms. Additionally, modification profiles of H4 acetylation were very similar among the organisms examined.
AB - Post-translational modifications (PTMs) of histones play an important role inmanycellular processes, notably gene regulation. Using a combination of mass spectrometric and immunobiochemical approaches, we show that the PTM profile of histone H3 differs significantly among the various model organisms examined. Unicellular eukaryotes, such as Saccharomyces cerevisiae (yeast) and Tetrahymena thermophila (Tet), for example, contain more activation than silencing marks as compared with mammalian cells (mouse and human), which are generally enriched in PTMs more often associated with gene silencing. Close examination reveals that many of the better-known modified lysines (Lys) can be either methylated or acetylated and that the overall modification patterns become more complex from unicellular eukaryotes to mammals. Additionally, novel species-specific H3 PTMs from wild-type asynchronously grown cells are also detected by mass spectrometry. Our results suggest that some PTMs are more conserved than previously thought, including H3K9me1 and H4K20me2 in yeast and H3K27me1, -me2, and -me3 in Tet. On histone H4, methylation at Lys-20 showed a similar pattern as H3 methylation at Lys-9, with mammals containing more methylation than the unicellular organisms. Additionally, modification profiles of H4 acetylation were very similar among the organisms examined.
UR - http://www.scopus.com/inward/record.url?scp=34147177521&partnerID=8YFLogxK
U2 - 10.1074/jbc.M607900200
DO - 10.1074/jbc.M607900200
M3 - Article
C2 - 17194708
AN - SCOPUS:34147177521
SN - 0021-9258
VL - 282
SP - 7641
EP - 7655
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 10
ER -