MSL Complex Is Attracted to Genes Marked by H3K36 Trimethylation Using a Sequence-Independent Mechanism

In Drosophila, X chromosome dosage compensation requires the male-specific lethal (MSL) complex, which associates with actively transcribed genes on the single male X chromosome to upregulate transcription ∼2-fold. We found that on the male X chromosome, or when MSL complex is ectopically localized...

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Bibliographic Details
Published in:Molecular cell 2007-10, Vol.28 (1), p.121-133
Main Authors: Larschan, Erica, Alekseyenko, Artyom A., Gortchakov, Andrey A., Peng, Shouyong, Li, Bing, Yang, Pok, Workman, Jerry L., Park, Peter J., Kuroda, Mitzi I.
Format: Article
Language:English
Subjects:
Animals
DEVBIO
DNA
DNA Methylation
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Drosophila melanogaster - genetics
Drosophila melanogaster - physiology
Drosophila Proteins - genetics
Drosophila Proteins - metabolism
Female
Gene Expression Regulation
Histone-Lysine N-Methyltransferase - genetics
Histone-Lysine N-Methyltransferase - metabolism
Histones - genetics
Histones - metabolism
Male
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Nucleosomes - metabolism
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
Transcription Factors - genetics
Transcription Factors - metabolism
Transgenes
X Chromosome
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Summary:In Drosophila, X chromosome dosage compensation requires the male-specific lethal (MSL) complex, which associates with actively transcribed genes on the single male X chromosome to upregulate transcription ∼2-fold. We found that on the male X chromosome, or when MSL complex is ectopically localized to an autosome, histone H3K36 trimethylation (H3K36me3) is a strong predictor of MSL binding. We isolated mutants lacking Set2, the H3K36me3 methyltransferase, and found that Set2 is an essential gene in both sexes of Drosophila. In set2 mutant males, MSL complex maintains X specificity but exhibits reduced binding to target genes. Furthermore, recombinant MSL3 protein preferentially binds nucleosomes marked by H3K36me3 in vitro. Our results support a model in which MSL complex uses high-affinity sites to initially recognize the X chromosome and then associates with many of its targets through sequence-independent features of transcribed genes.
ISSN:1097-2765
1097-4164
DOI:10.1016/j.molcel.2007.08.011