PR Domain-containing Protein 7 (PRDM7) Is a Histone 3 Lysine 4 Trimethyltransferase*

التفاصيل البيبلوغرافية
العنوان: PR Domain-containing Protein 7 (PRDM7) Is a Histone 3 Lysine 4 Trimethyltransferase*
المؤلفون: Peter Loppnau, Elisa Gibson, Masoud Vedadi, Matthieu Schapira, Cheryl H. Arrowsmith, Evelyne Lima-Fernandes, Levi L. Blazer, Mohammad S. Eram
المصدر: The Journal of Biological Chemistry
بيانات النشر: American Society for Biochemistry and Molecular Biology, 2016.
سنة النشر: 2016
مصطلحات موضوعية: 0301 basic medicine, Methyltransferase, substrate specificity, Lysine, Mutation, Missense, Biochemistry, Methylation, Serine, Histones, 03 medical and health sciences, Gene Duplication, Histone methylation, Humans, histone modification, histone methylation, Tyrosine, Molecular Biology, PRDM9, biology, epigenetics, zinc finger, Cell Biology, Histone-Lysine N-Methyltransferase, 030104 developmental biology, Histone, HEK293 Cells, Amino Acid Substitution, Mutagenesis, Histone methyltransferase, biology.protein, Enzymology
الوصف: PR domain-containing protein 7 (PRDM7) is a primate-specific histone methyltransferase that is the result of a recent gene duplication of PRDM9. The two proteins are highly homologous, especially in the catalytic PR/SET domain, where they differ by only three amino acid residues. Here we report that PRDM7 is an efficient methyltransferase that selectively catalyzes the trimethylation of H3 lysine 4 (H3K4) both in vitro and in cells. Through selective mutagenesis we have dissected the functional roles of each of the three divergent residues between the PR domains of PRDM7 and PRDM9. These studies indicate that after a single serine to tyrosine mutation at residue 357 (S357Y), PRDM7 regains the substrate specificities and catalytic activities similar to its evolutionary predecessor, including the ability to efficiently methylate H3K36.
اللغة: English
تدمد: 1083-351X
0021-9258
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1144351be53db649355f9a3f3cb86787
http://europepmc.org/articles/PMC4919437
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....1144351be53db649355f9a3f3cb86787
قاعدة البيانات: OpenAIRE