Incorporation of the Noncoding <i>roX</i> RNAs Alters the Chromatin-Binding Specificity of the <i>Drosophila</i> MSL1/MSL2 Complex

Li, F; Schiemann, Anja; Scott, MJ

doi:10.1128/mcb.00309-08

Cited by 18 publications

(34 citation statements)

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“…Msl1 also binds to the histone acetytransferase Mof protein (Hilfiker et al, 1997), which acetylates histone H4 at lysine 16 on nucleosomes (Smith et al, 2000). Further assembly of the complex involves the association of Msl3 with Msl1, and the association of Mle, an ATP-dependent helicase, with both Msl2 and roX RNAs (Lucchesi et al, 2005;Li et al, 2005Li et al, , 2008. This complex assembles only in males because msl2 RNA is not translated in females (Kelley et al, 1997).…”

Section: Mutations In Dosage Compensation Loci Enhance the Vg-fbz Malmentioning

confidence: 99%

“…Importantly, a leucine zipper like-motif within Msl1 protein was demonstrated to mediate association with Msl2 (Li et al, 2005). This association appears to form the scaffold for binding other components of the dosage compensation complex, as well as for DNA binding (Lucchesi et al, 2005;Li et al, 2005Li et al, , 2008. Therefore, one hypothesis to explain the male phenotypes from Fos bZip expression involves interference with the assembly of the complex through effects on Msl1 or Msl2.…”

Section: Overexpression Of Wild-type and Mutant Forms Of Msl Proteinsmentioning

confidence: 99%

“…If Fos bZip elicits its effects through a perturbation of this interaction, then overexpression of Msl1 or Msl2 forms containing only amino terminal regions may modify the Fos bZip phenotype. We used heat shock-regulated transgenes carrying residues 1-265 of Msl1 and 1-193 of Msl2, which contain the polypeptide regions implicated in the Msl1-Msl2 physical association, to investigate this idea (Li et al, 2005(Li et al, , 2008. Significant enhancement of the Fos bZip phenotype was observed after expression of each truncated protein (44% vs. 67%; Table 3).…”

Section: Overexpression Of Wild-type and Mutant Forms Of Msl Proteinsmentioning

confidence: 99%

“…Enhancement was also seen after expression of a carboxy segment of Msl-2, containing residues 490-773 (44% vs. 74%; Table 3). Although this segment of Msl-2 is not implicated in the physical interaction with Msl-1, it has been shown to bind MLE and influence rox RNA function (Li et al, 2008). In contrast, expression of an Msl-1 protein deleted for the aminoterminal 84 amino acids (Msl-1⌬84) significantly rescued the Fos bZip phenotype (31% vs. 44%; Table 3).…”

Section: Overexpression Of Wild-type and Mutant Forms Of Msl Proteinsmentioning

confidence: 99%

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A male‐specific effect of dominant‐negative Fos

Pierre

Morra

Lucchesi

et al. 2008

Developmental Dynamics

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The transcription factor Fos contains a basic DNA binding domain combined with a leucine zipper (bZip). Expression of a truncated form of Fos in Drosophila that contains only the bZip region (Fos bZip) elicits phenotypes resembling fos mutations. These effects presumably derive from competition between wild-type and truncated forms for dimerization partners, with the truncation acting in a dominant-negative manner. We found that expression of Fos bZip elicits male-specific phenotypes. Moreover, genetic interactions occur between Fos bZip and mutations in loci encoding the X chromosome dosage compensation complex. Fos bZip effects are correlated with aberrant male X chromosome structure and depressed signaling through the X-linked Notch locus. Unexpectedly, the male-specific effects are not reproduced with Fos RNAi, suggesting that Fos bZip can be neomorphic in nature. These results provide insight into how mutations in bZip proteins can exhibit gain of function activity. Developmental Dynamics 237:3361-3372, 2008.

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Section: Mutations In Dosage Compensation Loci Enhance the Vg-fbz Malmentioning

confidence: 99%

Section: Overexpression Of Wild-type and Mutant Forms Of Msl Proteinsmentioning

confidence: 99%

Section: Overexpression Of Wild-type and Mutant Forms Of Msl Proteinsmentioning

confidence: 99%

Section: Overexpression Of Wild-type and Mutant Forms Of Msl Proteinsmentioning

confidence: 99%

See 2 more Smart Citations

A male‐specific effect of dominant‐negative Fos

Pierre

Morra

Lucchesi

et al. 2008

Developmental Dynamics

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“…The RNA helicase MLE colocalizes with MSL2 at HAS and facilitates the incorporation of roX into the complex. The RNA is important for the distribution of the MSL-DCC along the X-chromosome, where it activates target genes 2,[5][6][7] .…”

mentioning

confidence: 99%

UNR facilitates the interaction of MLE with the lncRNA roX2 during Drosophila dosage compensation

et al. 2014

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Dosage compensation is a regulatory process that balances the expression of X-chromosomal genes between males (XY) and females (XX). In Drosophila, this requires non-coding RNAs and RNA-binding proteins (RBPs) whose specific functions remain elusive. Here we show that the Drosophila RBP UNR promotes the targeting of the activating male-specific-lethal complex to the X-chromosome by facilitating the interaction of two crucial subunits: the RNA helicase MLE and the long non-coding RNA roX2.

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Transcription modulation chromosome-wide: universal features and principles of dosage compensation in worms and flies

Straub

Becker

2011

Current Opinion in Genetics & Development

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Incorporation of the Noncoding roX RNAs Alters the Chromatin-Binding Specificity of the Drosophila MSL1/MSL2 Complex

Cited by 18 publications

References 0 publications

A male‐specific effect of dominant‐negative Fos

A male‐specific effect of dominant‐negative Fos

UNR facilitates the interaction of MLE with the lncRNA roX2 during Drosophila dosage compensation

Transcription modulation chromosome-wide: universal features and principles of dosage compensation in worms and flies

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