MSL1 plays a central role in assembly of the MSL complex, essential for dosage compensation in Drosophila

In male Drosophila, histone H4 acetylated at Lys16 is enriched on the X chromosome, and most X‐linked genes are transcribed at a higher rate than in females (thus achieving dosage compensation). Five proteins, collectively called the MSLs, are required for dosage compensation and male viability. Her...

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Bibliographic Details
Published in:	The EMBO journal Vol. 19; no. 1; pp. 144 - 155
Main Authors:	Scott, M.J, Pan, L.L, Cleland, S.B, Knox, A.L, Heinrich, J
Format:	Journal Article
Language:	English
Published:	Chichester, UK John Wiley & Sons, Ltd 04-01-2000 Blackwell Publishing Ltd
Subjects:	acyltransferases Amino Acid Sequence Animals binding binding proteins CBP CBP protein Chromatography, Affinity Coloring Agents Compensation DNA-Binding Proteins - metabolism dosage compensation Dosage Compensation, Genetic Drosophila Drosophila melanogaster Drosophila melanogaster - genetics Drosophila Proteins Female FLAG affinity gel gene expression gene overexpression Heterozygote histone acetyltransferase Indoles interactions lethal genes Male male specific lethality male-specific lethal males Mice MOF protein Molecular Sequence Data MSL complex MSL1 protein MSL2 protein MSL3 protein mutants Nuclear Proteins - metabolism Nuclear Proteins - physiology Transcription Factors - metabolism Transcription Factors - physiology viability X chromosome X Chromosome - metabolism Zinc Fingers
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Summary:	In male Drosophila, histone H4 acetylated at Lys16 is enriched on the X chromosome, and most X‐linked genes are transcribed at a higher rate than in females (thus achieving dosage compensation). Five proteins, collectively called the MSLs, are required for dosage compensation and male viability. Here we show that one of these proteins, MSL1, interacts with three others, MSL2, MSL3 and MOF. The latter is a putative histone acetyl transferase. Overexpression of either the N‐ or C‐terminal domain of MSL1 has dominant‐negative effects, i.e. causes male‐specific lethality. The lethality due to expression of the N‐terminal domain is reduced if msl2 is co‐overexpressed. MSL2 co‐purifies over a FLAG affinity column with the tagged region of MSL1, and both MSL3 and MOF co‐purify with the FLAG‐tagged MSL1 C‐terminal domain. Furthermore, the MSL1 C‐terminal domain binds specifically to a GST–MOF fusion protein and co‐immunoprecipitates with HA‐tagged MSL3. The MSL1 C‐terminal domain shows similarity to a region of mouse CBP, a transcription co‐activator. We conclude that a main role of MSL1 is to serve as the backbone for assembly of the MSL complex.
Bibliography:	ark:/67375/WNG-G8C00C03-5 ArticleID:EMBJ7592124 istex:8294453639B9997649C3F8110541CAF28FED8F11 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0261-4189 1460-2075 1460-2075
DOI:	10.1093/emboj/19.1.144