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Structural Studies of Histone Methylation
Author(s) -
Xu RuiMing
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.424.1
Epigenetic control of gene expression involves alterations of higher order chromatin structure, which is governed by a number of factors including covalent modifications of histones. Structural studies of histone methyl transferases have played important roles in dissecting molecular mechanisms of epigenetic inheritance, ranging from the elucidation of enzymatic mechanisms of key histone modification enzymes to the revelation of structural basis for recognition of histone modifications. I will present our latest results in structural and biochemical analyses of several important histone methyltransferases, including both histone lysine and arginine methyltransferases. These results provide valuable insights into the molecular mechanisms of substrate specificity and regulation of these important enzymes.

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