Saturation transfer difference measurements with SU(VAR)3-9 and S-adenosyl-L-methionine.
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.
Seeger
Karsten
K
Institute of Analytical Chemistry, University of Leipzig, Johannisallee 29, D-04103 Leipzig, Germany.
Lein
Sandro
S
Reuter
Gunter
G
Berger
Stefan
S
D000818:Animals; D001665:Binding Sites; D029721:Drosophila Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000235:genetics / Q000378:metabolism; D066298:In Vitro Techniques; D007700:Kinetics; D008745:Methylation; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D012097:Repressor Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D012436:S-Adenosylmethionine / Q000737:chemistry / Q000378:metabolism*
D029721:Drosophila Proteins; D012097:Repressor Proteins; C089148:Su(var)3-9 protein, Drosophila; D012436:S-Adenosylmethionine