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Regulation of MLL1 H3K4 methyltransferase activity by its core components.

Abstract：

:Histone H3 Lys4 (H3K4) methylation is a prevalent mark associated with transcription activation. A common feature of several H3K4 methyltransferase complexes is the presence of three structural components (RbBP5, Ash2L and WDR5) and a catalytic subunit containing a SET domain. Here we report the first biochemical reconstitution of a functional four-component mixed-lineage leukemia protein-1 (MLL1) core complex. This reconstitution, combined with in vivo assays, allows direct analysis of the contribution of each component to MLL1 enzymatic activity and their roles in transcriptional regulation. Moreover, taking clues from a crystal structure analysis, we demonstrate that WDR5 mediates interactions of the MLL1 catalytic unit both with the common structural platform and with the histone substrate. Mechanistic insights gained from this study can be generalized to the whole family of SET1-like histone methyltransferases in mammals.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Dou Y,Milne TA,Ruthenburg AJ,Lee S,Lee JW,Verdine GL,Allis CD,Roeder RG

doi

10.1038/nsmb1128

subject

Has Abstract

pub_date

2006-08-01 00:00:00

pages

713-9

issue

8

eissn

1545-9993

issn

1545-9985

pii

nsmb1128

journal_volume

13

pub_type

杂志文章

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