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Molecular and Cellular Biology, October 2005, p. 8913-8924, Vol. 25, No. 20
0270-7306/05/$08.00+0 doi:10.1128/MCB.25.20.8913-8924.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Centre for Functional Genomics, Institute of Molecular BioSciences, Massey University, Private Bag 11222, Palmerston North, New Zealand,1 Institute of Fundamental Sciences, Massey University, Private Bag 11222, Palmerston North, New Zealand2
Received 23 March 2005/ Returned for modification 6 June 2005/ Accepted 18 July 2005
In Drosophila melanogaster, X chromosome dosage compensation is achieved by doubling the transcription of most X-linked genes. The male-specific lethal (MSL) complex is required for this process and binds to hundreds of sites on the male X chromosome. The MSL1 protein is essential for X chromosome binding and serves as a central scaffold for MSL complex assembly. We find that the amino-terminal region of MSL1 binds to hundreds of sites on the X chromosome in normal males but only to approximately 30 high-affinity sites in the absence of endogenous MSL1. Binding to the high-affinity sites requires a basic motif at the amino terminus that is conserved among Drosophila species. X chromosome binding also requires a conserved leucine zipper-like motif that binds to MSL2. A glycine-rich motif between the basic and leucine-zipper-like motifs mediates MSL1 self-association in vitro and binding of the amino-terminal region of MSL1 to the MSL complex assembled on the male X chromosome. We propose that the basic region may mediate DNA binding and that the glycine-rich region may promote the association of MSL complexes to closely adjacent sites on the X chromosome.
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