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Molecular and Cellular Biology, February 2008, p. 1252-1264, Vol. 28, No. 4
0270-7306/08/$08.00+0 doi:10.1128/MCB.00910-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
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Centre for Functional Genomics, Institute of Molecular BioSciences, Massey University, Palmerston North, New Zealand
Received 22 May 2007/ Returned for modification 25 June 2007/ Accepted 4 December 2007
The male-specific lethal (MSL) protein-RNA complex is required for X chromosome dosage compensation in Drosophila melanogaster. The MSL2 and MSL1 proteins form a complex and are essential for X chromosome binding. In addition, the MSL complex must integrate at least one of the noncoding roX RNAs for normal X chromosome binding. Here we find the amino-terminal RING finger domain of MSL2 binds as a complex with MSL1 to the heterochromatic chromocenter and a few sites on the chromosome arms. This binding required the same amino-terminal basic motif of MSL1 previously shown to be essential for binding to high-affinity sites on the X chromosome. While the RING finger domain of MSL2 is sufficient to increase the expression of roX1 in females, activation of roX2 requires motifs in the carboxyl-terminal domain. Binding to hundreds of sites on the X chromosome and efficient incorporation of the roX RNAs into the MSL complex require proline-rich and basic motifs in the carboxyl-terminal domain of MSL2. We suggest that incorporation of the roX RNAs into the MSL complex alters the binding specificity of the chromatin-binding module formed by the amino-terminal domains of MSL1 and MSL2.
Published ahead of print on 17 December 2007.
Supplemental material for this article may be found at http://mcb.asm.org/.
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