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Structural analysis of lysine‐4 methylated histone H3 proteins using synchrotron radiation circular dichroism spectroscopy
Author(s) -
Izumi Yudai,
Matsuo Koichi,
Namatame Hirofumi
Publication year - 2018
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.22849
Subject(s) - chemistry , circular dichroism , synchrotron radiation , lysine , vibrational circular dichroism , spectroscopy , histone h3 , histone , crystallography , biochemistry , dna , amino acid , optics , physics , quantum mechanics
We report structural alterations of histone H3 proteins induced by lysine‐4 (K4) monomethylation, dimethylation, and trimethylation identified by using synchrotron radiation circular dichroism spectroscopy. Compared with unmethylated H3, monomethylation and dimethylation induced increases in α‐helix structures and decreases in β‐strand structures. In contrast, trimethylation decreased α‐helix content but increased β‐strand content. The structural differences among K4‐unmethylated/methylated H3 may allow epigenetic enzymes to discriminate the substrates both chemically and sterically.