Molecular and Cellular Biology, July 2005, p. 5947-5954, Vol. 25, No. 14
0270-7306/05/$08.00+0 doi:10.1128/MCB.25.14.5947-5954.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
The MRG Domain Mediates the Functional Integration of MSL3 into the Dosage Compensation Complex
Violette Morales,
Catherine Regnard,
Annalisa Izzo,
Irene Vetter, and
Peter B. Becker*
Adolf-Butenandt-Institut, Molekularbiologie, Schillerstr. 44, 80336 München, Germany
Received 23 January 2004/
Returned for modification 13 January 2005/
Accepted 29 April 2005
The male-specific-lethal (MSL) proteins in Drosophila melanogaster serve to adjust gene expression levels in male flies containing a single X chromosome to equal those in females with a double dose of X-linked genes. Together with noncoding roX RNA, MSL proteins form the "dosage compensation complex" (DCC), which interacts selectively with the X chromosome to restrict the transcription-activating histone H4 acetyltransferase MOF (males-absent-on-the-first) to that chromosome. We showed previously that MSL3 is essential for the activation of MOF's nucleosomal histone acetyltransferase activity within an MSL1-MOF complex. By characterizing the MSL3 domain structure and its associated functions, we now found that the nucleic acid binding determinants reside in the N terminus of MSL3, well separable from the C-terminal MRG signatures that form an integrated domain required for MSL1 interaction. Interaction with MSL1 mediates the activation of MOF in vitro and the targeting of MSL3 to the X-chromosomal territory in vivo. An N-terminal truncation that lacks the chromo-related domain and all nucleic acid binding activity is able to trigger de novo assembly of the DCC and establishment of an acetylated X-chromosome territory.
* Corresponding author. Mailing address: Adolf-Butenandt-Institut, Molekularbiologie, Schillerstr. 44, 80336 München, Germany. Phone: 49-89-2180-75428. Fax: 49-89-2180-75425. E-mail: pbecker{at}med.uni-muenchen.de.
Present address: Laboratoire de Biologie Moléculaire des Eucaryotes, LBME-CNRS UMR 5099-IFR 109, Université Paul Sabatier, 118 Route de Narbonne, 31062-Toulouse Cedex, France.
Molecular and Cellular Biology, July 2005, p. 5947-5954, Vol. 25, No. 14
0022-538X/05/$08.00+0 doi:10.1128/MCB.25.14.5947-5954.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
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Copyright © 2005 by the American Society for Microbiology. All rights reserved.