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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Complex formation by the Drosophila MSL proteins: role of the MSL2 RING finger in protein complex assembly.

Drosophila MSL proteins are thought to act within a complex to elevate transcription from the male X chromosome. We found that the MSL1, MSL2 and MSL3 proteins are associated in immunoprecipitations, chromatographic steps and in the yeast two-hybrid system, but that the MLE protein is not tightly complexed in these assays. We focused our analysis on the MSL2- MSL1 interaction, which is postulated to play a critical role in MSL complex association with the X chromosome. Using a modified two-hybrid assay, we isolated missense mutations in MSL2 that disrupt its interaction with MSL1. Eleven out of 12 mutated residues clustered around the first zinc-binding site of the RING finger domain were conserved in a Drosophila virilis MSL2 homolog. Two pre-existing msl2 alleles, which fail to support male viability in vivo, have lesions in the same region of the RING finger. We tested these in the two-hybrid system and found that they are also defective in interaction with MSL1. Mutation of the second zinc-binding site had little effect on MSL1 binding, suggesting that this portion of the RING finger may have a distinct function. Our data support a model in which MSL2- MSL1 interaction nucleates assembly of an MSL complex, with which MLE is weakly or transiently associated.[1]


  1. Complex formation by the Drosophila MSL proteins: role of the MSL2 RING finger in protein complex assembly. Copps, K., Richman, R., Lyman, L.M., Chang, K.A., Rampersad-Ammons, J., Kuroda, M.I. EMBO J. (1998) [Pubmed]
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