This paper uses a "bump and hole" approach to study a vSET methyltransferase mutant and SAM analog pair. This pair is responsible for histone methylation and affects gene transcription. To create the "bumped" SAM analog (16c) and "hole" protein (vSET-L116A), the crystal structure was used. The vSET-L116A/16c combination was shown to have decreased activity as compared to wild type/SAM and mutant/SAM combinations.
Tuesday, October 18, 2011
Structure-Guided Design of a Methyl Donor Cofactor That Controls a Viral Histone H3 Lysine 27 Methyltransferase Activity
This paper uses a "bump and hole" approach to study a vSET methyltransferase mutant and SAM analog pair. This pair is responsible for histone methylation and affects gene transcription. To create the "bumped" SAM analog (16c) and "hole" protein (vSET-L116A), the crystal structure was used. The vSET-L116A/16c combination was shown to have decreased activity as compared to wild type/SAM and mutant/SAM combinations.
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ReplyDeleteLast line should be corrected to:
ReplyDelete"The vSET-L116A/16c combination was shown to have similar activity as compared to wild type/SAM and increased activity compared to wild type/16c combination."
They say vSET can specifically methylate H3K27 in eukaryotic cells. This obviously wouldn't be that useful if it methylates all the nucleosomes (and therefore turns off gene expression for all genes). I wonder if it methylates the same ones that the native PRC2 complex methylates at a given time.
ReplyDeleteI think vSET only methylates histone H3 lysine 27, therefore, I wouldn't think it completely turns off all gene expression. But, having a tool, such as the bump/hole system, that can control transcription would be great to study specific genes.
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