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Chemical synthesis of the ubiquitinated form of histone H3 and its effect on DNA methyltransferase 1
Author(s) -
Kawakami Toru,
Mishima Yuichi,
Takazawa Masaya,
Hojo Hironobu,
Suetake Isao
Publication year - 2019
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3200
Subject(s) - ubiquitin , histone , histone h2a , nucleosome , histone methyltransferase , histone h3 , biochemistry , chemistry , histone h1 , histone code , microbiology and biotechnology , dna , biology , gene
Posttranslational modifications of histone proteins, which form nucleosome cores, play an important role in gene regulation. Ubiquitination is one such modification. We previously reported on the synthesis of ubiquitinated histone H3 with an isopeptide mimetic structure. In this report, we describe the preparation of ubiquitinated histone H3 peptides with a native isopeptide structure, which showed a slightly weaker effect on the enzymatic activity of DNA methyltransferase 1 than the previous ubiquitinated H3 peptide analogs. These findings show that a native structure is important for determining the mechanism of the function, although ubiquitinated H3 peptide analogs can mimic the role of the original ubiquitinated H3. We also report on the successful preparation of the ubiquitinated full length histone H3.