Abstract:
:Dot1 is an evolutionarily conserved histone methyltransferase that methylates lysine-79 of histone H3 in the core domain. Unlike other histone methyltransferases, Dot1 does not contain a SET domain, and it specifically methylates nucleosomal histone H3. We have solved a 2.5 A resolution structure of the catalytic domain of human Dot1, hDOT1L, in complex with S-adenosyl-L-methionine (SAM). The structure reveals a unique organization of a mainly alpha-helical N-terminal domain and a central open alpha/beta structure, an active site consisting of a SAM binding pocket, and a potential lysine binding channel. We also show that a flexible, positively charged region at the C terminus of the catalytic domain is critical for nucleosome binding and enzymatic activity. These structural and biochemical analyses, combined with molecular modeling, provide mechanistic insights into the catalytic mechanism and nucleosomal specificity of Dot1 proteins.
journal_name
Celljournal_title
Cellauthors
Min J,Feng Q,Li Z,Zhang Y,Xu RMdoi
10.1016/s0092-8674(03)00114-4subject
Has Abstractpub_date
2003-03-07 00:00:00pages
711-23issue
5eissn
0092-8674issn
1097-4172pii
S0092867403001144journal_volume
112pub_type
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