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Structural biology of human H3K9 methyltransferases

Wu, Hong ; Min, Jinrong ; Lunin, Vladimir V ; Antoshenko, Tatiana ; Dombrovski, Ludmila ; Zeng, Hong ; Allali-Hassani, Abdellah ; Campagna-Slater, Valérie ; Vedadi, Masoud ; Arrowsmith, Cheryl H ; Plotnikov, Alexander N ; Schapira, Matthieu Gay, Nick

PloS one, 2010-01, Vol.5 (1), p.e8570-e8570 [Periódico revisado por pares]

United States: Public Library of Science

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Título:
Structural biology of human H3K9 methyltransferases
Autor: Wu, Hong ; Min, Jinrong ; Lunin, Vladimir V ; Antoshenko, Tatiana ; Dombrovski, Ludmila ; Zeng, Hong ; Allali-Hassani, Abdellah ; Campagna-Slater, Valérie ; Vedadi, Masoud ; Arrowsmith, Cheryl H ; Plotnikov, Alexander N ; Schapira, Matthieu
Gay, Nick
Assuntos: Analysis ; Arginine ; Biochemistry ; Biochemistry/Protein Chemistry ; Biochemistry/Structural Genomics ; Catalysis ; Catalytic Domain ; Conformation ; Consortia ; Crystallization ; Docking ; Electrostatic properties ; Electrostatics ; Enzymes ; Epigenetic inheritance ; Epigenetics ; Gene expression ; Gene regulation ; Genetic aspects ; Genetics and Genomics/Epigenetics ; Genomics ; Histone-Lysine N-Methyltransferase - chemistry ; Humans ; Lysine ; Methylation ; Methyltransferases ; Models, Molecular ; Peptides ; Protein Conformation ; Proteins ; Static Electricity ; Substrate Specificity ; Substrates ; Transcription
É parte de: PloS one, 2010-01, Vol.5 (1), p.e8570-e8570
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Current address: Department of Structural and Chemical Biology, Icahn Medical Institute, Mount Sinai School of Medicine, New York, New York, United States of America
Conceived and designed the experiments: HW MV AP. Performed the experiments: HW JM VVL TA LD HZ AAH VCS. Analyzed the data: HW CHA AP MS. Wrote the paper: MS.
Descrição: SET domain methyltransferases deposit methyl marks on specific histone tail lysine residues and play a major role in epigenetic regulation of gene transcription. We solved the structures of the catalytic domains of GLP, G9a, Suv39H2 and PRDM2, four of the eight known human H3K9 methyltransferases in their apo conformation or in complex with the methyl donating cofactor, and peptide substrates. We analyzed the structural determinants for methylation state specificity, and designed a G9a mutant able to tri-methylate H3K9. We show that the I-SET domain acts as a rigid docking platform, while induced-fit of the Post-SET domain is necessary to achieve a catalytically competent conformation. We also propose a model where long-range electrostatics bring enzyme and histone substrate together, while the presence of an arginine upstream of the target lysine is critical for binding and specificity. This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.
Editor: United States: Public Library of Science
Idioma: Inglês

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Structural biology of human H3K9 methyltransferases

Wu, Hong ; Min, Jinrong ; Lunin, Vladimir V ; Antoshenko, Tatiana ; Dombrovski, Ludmila ; Zeng, Hong ; Allali-Hassani, Abdellah ; Campagna-Slater, Valérie ; Vedadi, Masoud ; Arrowsmith, Cheryl H ; Plotnikov, Alexander N ; Schapira, Matthieu Gay, Nick

United States: Public Library of Science

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