Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11535-40. Epub 2003 Sep 17.

ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3.

Author information

  • 1Department of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.

Abstract

Covalent modifications of histone tails modulate gene expression via chromatin organization. As examples, methylation of lysine 9 residues of histone H3 (H3) (H3-K9) is believed to repress transcription by compacting chromatin, whereas methylation of lysine 4 residues of H3 (H3-K4) is believed to activate transcription by relaxing chromatin. The Drosophila trithorax group protein absent, small, or homeotic discs 1 (ASH1) is involved in maintaining active transcription of many genes. Here we report that in extreme ash1 mutants, no H3-K4 methylation is detectable. Within the limits of our assays, this lack of detectable H3-K4 methylation implies that ASH1 is required for essentially all H3-K4 methylation that occurs in vivo. We report further that the 149-aa SET domain of ASH1 is sufficient for H3-K4 methylation in vitro. These findings support a model in which ASH1 is directly involved in maintaining active transcription by conferring a relaxed chromatin structure.

PMID:
13679578
[PubMed - indexed for MEDLINE]
PMCID:
PMC208793
Free PMC Article

Images from this publication.See all images (5)Free text

Fig. 1.
Fig. 2.
Fig. 3.
Fig. 4.
Fig. 5.
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk