Drosophila male-specific lethal-2 protein: structure/function analysis and dependence on MSL-1 for chromosome association

• Published in: Genetics (Austin) 1997-12, Vol.147 (4), p.1743-1753
• Main Authors: Lyman, L.M. (Baylor College of Medicine, Houston, TX.), Copps, K, Rastelli, L, Kelley, R.L, Kuroda, M.I
• Format: Article
• Language: English
• Subjects: ADN; ALLELES; Amino Acid Sequence; ANIMAL TRANSGENIQUE; ANIMALES TRANSGENICOS; Animals; BINDING; BINDING PROTEINS; CHROMOSOME; Chromosome Mapping; CHROMOSOMES; CROMOSOMAS; Cysteine - metabolism; DNA; DNA BINDING MOTIFS; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; DOMINANT SUPPRESSORS; DROSOPHILA MELANOGASTER; Drosophila melanogaster - genetics; Drosophila melanogaster - metabolism; Drosophila Proteins; EXPRESION GENICA; EXPRESSION DES GENES; Female; FEMALES; FEMELLE; FENOTIPOS; GENE; GENE EXPRESSION; GENES; Genetics; HEMBRA; INDUCED MUTATION; INHIBITOR GENES; Insects; INTERACTIONS; Investigations; MACHO; MALE; MALES; Molecular Sequence Data; MUTACION; MUTACION INDUCIDA; Mutagenesis; MUTANT; MUTANTES; MUTANTS; MUTATION; MUTATION PROVOQUEE; Nuclear Proteins - chemistry; Nuclear Proteins - genetics; Nuclear Proteins - metabolism; PHENOTYPE; PHENOTYPES; PROTEINAS AGLUTINANTES; PROTEINE DE LIAISON; Proteins; Structure-Activity Relationship; TARGETED MUTAGENESIS; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - metabolism; TRANSGENIC ANIMALS; X CHROMOSOME; Zinc Fingers
• ISSN: 0016-6731; 1943-2631

MSL-2 is required for the male-specific assembly of a dosage compensation regulatory complex on the X chromosome of Drosophila melanogaster. We found that MSL-2 binds in a reproducible, partial pattern to the male X chromosome in the absence of MLE or MSL-3, or when ectopically expressed at a low level in females. Moreover, the pattern of MSL-2 binding corresponds precisely in each case to that of MSL-1, suggesting that the two proteins function together to associate with the X. Consistent with this hypothesis, we isolated EMS-induced loss of function msl-1 and msl-2 alleles in a screen for suppressors of the toxic effects of MSL-2 expression in females. We also used site-directed mutagenesis to determine the importance of the MSL-2 RING finger domain and second cysteine-rich motif. The mutations, including those in conserved zinc coordinating cysteines, confirm that the RING finger is essential for MSL-2 function, while suggesting a less stringent requirement for an intact second motif.