Abstract
Saturation transfer difference NMR measurements were performed to investigate the interaction of S-adenosyl-l-methionine (AdoMet) with SU(VAR)3-9 from Drosophila melanogaster. SU(VAR)3-9 has a SET domain and plays an important role in methylation of lysine-9 of histone H3 which results in gene silencing. We determined the binding epitope of AdoMet and compared it with a crystal structure of another SET protein.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Binding Sites
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Drosophila Proteins / chemistry*
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Drosophila Proteins / genetics
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Drosophila Proteins / metabolism*
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Drosophila melanogaster / genetics
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Drosophila melanogaster / metabolism
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In Vitro Techniques
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Kinetics
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Methylation
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Models, Molecular
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Nuclear Magnetic Resonance, Biomolecular
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Protein Conformation
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Repressor Proteins / chemistry*
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Repressor Proteins / genetics
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Repressor Proteins / metabolism*
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S-Adenosylmethionine / chemistry
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S-Adenosylmethionine / metabolism*
Substances
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Drosophila Proteins
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Repressor Proteins
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Su(var)3-9 protein, Drosophila
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S-Adenosylmethionine