TY - JOUR
T1 - Post-translational modifications of the N-terminal tail of histone H3 in holocentric chromosomes of Bombyx mori
AU - Mon, Hiroaki
AU - Izumi, Makiko
AU - Mitsunobu, Hitoshi
AU - Tatsuke, Tsuneyuki
AU - Iiyama, Kazuhiro
AU - Jikuya, Hiroyuki
AU - Lee, Jae Man
AU - Kusakabe, Takahiro
N1 - Funding Information:
This work was supported in part by the Program for Promotion of Basic Research Activities for Innovative Biosciences (PROBRAIN), by a grant from the Ministry of Agriculture, Forestry and Fisheries of Japan (Integrated research project for plant, insect and animal using genome technology INSECT-1201), and KAKENHI no. 22248004 from the Japan Society for the Promotion of Science .
PY - 2011/11
Y1 - 2011/11
N2 - Epigenetic information is encoded in post-translational modifications (PTMs) of histones. Various combinations of these marks contribute to the regulation of chromatin-templated DNA metabolisms. The histone code is gradually translated into biological responses in model organisms. However, in the silkworm, the modifications of histones with unique holocentric chromosomes have not yet been analyzed. TAU-PAGE analysis of the silkworm histone variants H2A, H2B, and H3, separated by RP-HPLC, suggested silkworm specific modification. Detailed mass spectrometry analyses of the peptides derived from the N-terminus of the silkworm H3.2 generated by glutamyl endopeptidase, lysyl endopeptidase, and trypsin digestions revealed global modifications around H3K9.
AB - Epigenetic information is encoded in post-translational modifications (PTMs) of histones. Various combinations of these marks contribute to the regulation of chromatin-templated DNA metabolisms. The histone code is gradually translated into biological responses in model organisms. However, in the silkworm, the modifications of histones with unique holocentric chromosomes have not yet been analyzed. TAU-PAGE analysis of the silkworm histone variants H2A, H2B, and H3, separated by RP-HPLC, suggested silkworm specific modification. Detailed mass spectrometry analyses of the peptides derived from the N-terminus of the silkworm H3.2 generated by glutamyl endopeptidase, lysyl endopeptidase, and trypsin digestions revealed global modifications around H3K9.
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U2 - 10.1016/j.ibmb.2011.08.004
DO - 10.1016/j.ibmb.2011.08.004
M3 - Article
C2 - 21914479
AN - SCOPUS:80053132373
SN - 0965-1748
VL - 41
SP - 902
EP - 908
JO - Insect Biochemistry and Molecular Biology
JF - Insect Biochemistry and Molecular Biology
IS - 11
ER -