A prototypic lysine methyltransferase 4 from archaea with degenerate sequence specificity methylates chromatin proteins Sul7d and Cren7 in different patterns.

ABSTRACT:

Background

The origin of eukaryotic histone modification enzymes still remains obscure.

Results

Prototypic KMT4/Dot1 from Archaea targets chromatin proteins (Sul7d and Cren7) and shows increased activity on Sul7d, but not Cren7, in the presence of DNA.

Conclusion

Promiscuous aKMT4 could be regulated by chromatin environment.

Significance

This study supports the prokaryotic origin model of eukaryotic histone methyltransferases and sheds light on chromatin dynamics in Archaea. Histone methylation is one of the major epigenetic modifications even in early diverging unicellular eukaryotes. We show that a widespread lysine methyltransferase from Archaea (aKMT4), bears striking structural and functional resemblance to the core of distantly related eukaryotic KMT4/Dot

SUBMITTER: Niu Y 

PROVIDER: S-EPMC3650410 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature