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Male-specific lethal 3

MSL-3, MSL3L1
This gene encodes a nuclear protein that is similar to the product of the Drosophila male-specific lethal-3 gene. The Drosophila protein plays a critical role in a dosage-compensation pathway, which equalizes X-linked gene expression in males and females. Thus, the human protein is thought to play a similar function in chromatin remodeling and transcriptional regulation, and it has been found as part of a complex that is responsible for histone H4 lysine-16 acetylation. This gene can undergo X inactivation. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 2, 7 and 8. [provided by RefSeq, Jul 2010] (from NCBI)
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Top mentioned proteins: msl-2, MOF, Histone, CAN, H4
Papers using MSL-3 antibodies
Mitotic chromosome structure: reproducibility of folding and symmetry between sister chromatids.
Supplier
Misteli Tom, In PLoS Biology, 2008
... Fly line msl3-gfp, His2AvDmRFP1; msl3-gfp was created by recombination of msl3-gfp; msl3-gfp with a His2AvDmRFP1 transgenic line ...
Papers on MSL-3
Primary Sex Determination in Drosophila melanogaster Does Not Rely on the Male Specific Lethal (MSL) Complex.
New
Erickson, United States. In Genetics, Dec 2015
UNASSIGNED: It has been proposed that the Male Specific Lethal (MSL) complex is active in Drosophila melanogaster embryos of both sexes prior to the maternal to zygotic transition.
Proximity ligation assays of protein and RNA interactions in the male-specific lethal complex on Drosophila melanogaster polytene chromosomes.
New
Larsson et al., Umeå, Sweden. In Chromosoma, Sep 2015
Our results also indicate that JIL1, a histone H3 Ser10 kinase enriched on the male X chromosome, interacts with MSL1 and MSL2, but not MSL3 of the MSL complex.
Genetic architecture and functional characterization of genes underlying the rapid diversification of male external genitalia between Drosophila simulans and Drosophila mauritiana.
New
Nunes et al., Oxford, United Kingdom. In Genetics, May 2015
We found that six of these genes, including components of Wnt signaling and male-specific lethal 3 (msl3), regulate the development of genital traits consistent with the effects of the introgressed regions where they are located and that thus represent promising candidate genes for the evolution these traits.
RNA Sequencing Analysis of the msl2msl3, crl, and ggps1 Mutants Indicates that Diverse Sources of Plastid Dysfunction Do Not Alter Leaf Morphology Through a Common Signaling Pathway.
Haswell et al., Edwardsville, United States. In Front Plant Sci, 2014
As an alternative to the construction of higher-order mutants, we used contemporary expression profiling methods to perform pathway analysis on several Arabidopsis thaliana mutants, including the mscS-like (msl)2msl3 double mutant.
A screen for F1 hybrid male rescue reveals no major-effect hybrid lethality loci in the Drosophila melanogaster autosomal genome.
Barbash et al., Ithaca, United States. In G3 (bethesda), 2014
We attempted to test one candidate, the dosage compensation gene male specific lethal-3 (msl-3), by using RNA interference with short hairpin microRNA constructs targeted specifically against D. simulans msl-3 but failed to achieve knockdown, in part due to off-target effects.
Modulation of Heterochromatin by Male Specific Lethal Proteins and roX RNA in Drosophila melanogaster Males.
Meller et al., Detroit, United States. In Plos One, 2014
A subset of MSL complex proteins, including MSL1 and MSL3, is also necessary for full expression of autosomal heterochromatic genes in males, but not females.
Plastid osmotic stress activates cellular stress responses in Arabidopsis.
Haswell et al., Saint Louis, United States. In Plant Physiol, 2014
We have previously shown that Arabidopsis (Arabidopsis thaliana) plants lacking functional versions of the plastid-localized mechanosensitive ion channels Mechanosensitive Channel of Small Conductance-Like2 (MSL2) and MSL3 contain leaf epidermal plastids under hypoosmotic stress, even during normal growth and development.
Identifying candidate oocyte reprogramming factors using cross-species global transcriptional analysis.
Byrne et al., Los Angeles, United States. In Cell Reprogram, 2013
In this study, we have identified eight CORFs (ARID2, ASF1A, ASF1B, DPPA3, ING3, MSL3, H1FOO, and KDM6B) based on unbiased global transcriptional analysis of oocytes from three different species (human, rhesus monkey, and mouse) that both demonstrate significant (p<0.05,
Different chromatin interfaces of the Drosophila dosage compensation complex revealed by high-shear ChIP-seq.
Becker et al., München, Germany. In Genome Res, 2013
In contrast, association of the DCC with actively transcribed gene bodies is mediated by MSL-3 binding to nucleosomes.
[Research advance of dosage compensation and MSL complex].
Review
Zhang et al., Xiamen, China. In Yi Chuan, 2012
In Drosophila, the male-specific lethal (MSL) complex mediates dosage compensation by acetylating histone H4 lysine K16 on nucleosome of some specific sites on the male X chromosome, globally upregulates twofold expression of active X-linked genes from the single X chromosome, and makes up for the shortage that the male has only one single X chromosome in male Drosophila.
Mechanosensitive channels protect plastids from hypoosmotic stress during normal plant growth.
GeneRIF
Haswell et al., Saint Louis, United States. In Curr Biol, 2012
We conclude that plastids are under hypoosmotic stress during normal plant growth and dynamic response to this stress requires MSL2 and MSL3.
Two mechanosensitive channel homologs influence division ring placement in Arabidopsis chloroplasts.
GeneRIF
Haswell et al., Saint Louis, United States. In Plant Cell, 2011
MSL2, MSL3, and components of the Min system function in the same pathway to regulate chloroplast size and FtsZ ring formation.
Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1.
GeneRIF
Akhtar et al., Grenoble, France. In Nat Struct Mol Biol, 2011
Msl1 interacts with Msl3 as an extended chain forming an extensive hydrophobic interface, whereas the Msl1-MOF interface involves electrostatic interactions between the HAT domain and a long helix of Msl1.
Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4.
GeneRIF
Scott et al., Saskatoon, Canada. In J Biol Chem, 2011
MSL3 plays an important role in targeting the male specific lethal complex to chromatin in both humans and flies by binding to H4K20Me(1).
Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain.
GeneRIF
Khorasanizadeh et al., Charlottesville, United States. In Nat Struct Mol Biol, 2010
A DNA-dependent interaction of MSL3 chromodomain with the H4 lysine20 monomethyl mark, was discovered.
Genome-wide analysis reveals MOF as a key regulator of dosage compensation and gene expression in Drosophila.
Impact
Akhtar et al., Heidelberg, Germany. In Cell, 2008
Dosage compensation, mediated by the MSL complex, regulates X-chromosomal gene expression in Drosophila.
Path to equality strewn with roX.
Review
Kelley, Houston, United States. In Dev Biol, 2004
This is mediated by chromatin modifications carried out by the MSL complex composed of noncoding roX RNA and at least five MSL proteins.
Chromodomains are protein-RNA interaction modules.
Impact
Becker et al., München, Germany. In Nature, 2000
In vitro analyses of the MOF and MSL-3 chromodomains indicate that these chromodomains may function as RNA interaction modules.
Epigenetic spreading of the Drosophila dosage compensation complex from roX RNA genes into flanking chromatin.
Impact
Kuroda et al., Houston, United States. In Cell, 1999
When either msl3, mle, or mof is mutant, a partial MSL complex is bound at only approximately 35 unusual sites distributed along the X.
Regulation of the sex-specific binding of the maleless dosage compensation protein to the male X chromosome in Drosophila.
Impact
Baker et al., Stanford, United States. In Cell, 1993
Additionally, we have found that mle X chromosome binding requires wild-type msl1, msl2, and msl3 functions.
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