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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Male-specific lethal 2

Top mentioned proteins: MSL-3, Histone, MOF, CAN, MNT
Papers on msl-2
Improved accuracy from joint X-ray and NMR refinement of a protein-RNA complex structure.
Luchinat et al., In J Am Chem Soc, Feb 2016
Here, we refined the structure of a ternary protein-protein-RNA complex comprising three domains, Sxl and Unr, bound to a single-stranded region derived in the msl2 mRNA.
Primary Sex Determination in Drosophila melanogaster Does Not Rely on the Male Specific Lethal (MSL) Complex.
Erickson, United States. In Genetics, Dec 2015
Published data cited as evidence for an early function of the MSL complex in females, including a maternal effect of msl2, have been reevaluated and found not to support a maternal, or other effect, of the MSL complex in sex determination.
Proximity ligation assays of protein and RNA interactions in the male-specific lethal complex on Drosophila melanogaster polytene chromosomes.
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.
Structural basis of X chromosome DNA recognition by the MSL2 CXC domain during Drosophila dosage compensation.
Ye et al., Beijing, China. In Genes Dev, 2015
The male-specific lethal dosage compensation complex (MSL-DCC) selectively assembles on the X chromosome in Drosophila males and activates gene transcription by twofold through histone acetylation.
X-to-autosome expression and msl-2 transcript abundance correlate among Drosophila melanogaster somatic tissues.
Stone et al., Raleigh, United States. In Peerj, 2014
Specifically, we find X-to-autosome expression correlates with the tissue-specific expression of msl-2 which encodes an essential male-specific component of the MSL complex.
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.
Structural basis for the assembly of the Sxl-Unr translation regulatory complex.
Sattler et al., München, Germany. In Nature, 2014
In the fruitfly Drosophila melanogaster, the dosage-compensation complex promotes twofold hypertranscription of the single male X-chromosome and is silenced in females by inhibition of the translation of msl2, which codes for the limiting component of the dosage-compensation complex.
H2B ubiquitylation promotes RNA Pol II processivity via PAF1 and pTEFb.
Dou et al., Ann Arbor, United States. In Mol Cell, 2014
Knocking down MSL2 in the MOF-MSL complex affects not only global H2BK34ub, but also multiple cotranscriptionally regulated histone modifications.
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.
The MDM2 gene family.
Momand et al., In Biomol Concepts, 2014
Other RING domain E3 ubiquitin ligases that target p53 are COP1, Pirh2, and MSL2.
Mechanosensitive channels protect plastids from hypoosmotic stress during normal plant growth.
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.
msl2 mRNA is bound by free nuclear MSL complex in Drosophila melanogaster.
Larsson et al., Umeå, Sweden. In Nucleic Acids Res, 2011
A model is proposed in which a non-chromatin-associated partial or complete MSL-complex titrates newly transcribed msl2 mRNA and thus regulates the amount of available MSL complex by feedback.
Two mechanosensitive channel homologs influence division ring placement in Arabidopsis chloroplasts.
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.
The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation.
Dou et al., Ann Arbor, United States. In Mol Cell, 2011
MSL2, together with MSL1, has robust histone ubiquitylation activity that mainly targets nucleosomal H2B on lysine 34.
Translational control via protein-regulated upstream open reading frames.
Hentze et al., Heidelberg, Germany. In Cell, 2011
Analysis of the regulation of msl-2 mRNA by Sex lethal (SXL), which is critical for dosage compensation in Drosophila, has uncovered a mode of translational control based on common 5' untranslated region elements, upstream open reading frames (uORFs), and interaction sites for RNA-binding proteins.
The DNA binding CXC domain of MSL2 is required for faithful targeting the Dosage Compensation Complex to the X chromosome.
Becker et al., München, Germany. In Nucleic Acids Res, 2010
Reporter gene assays and localization of GFP-fusion proteins confirm the important contribution of the CXC domain of MSL2 for Dosage Compensation Complex targeting in vivo.
A dual inhibitory mechanism restricts msl-2 mRNA translation for dosage compensation in Drosophila.
Hentze et al., Heidelberg, Germany. In Cell, 2005
Here, we uncover the mechanism by which SXL achieves tight control of msl-2 translation initiation. This failsafe mechanism thus forms the molecular basis of a critical step in dosage compensation.
Inhibition of msl-2 splicing by Sex-lethal reveals interaction between U2AF35 and the 3' splice site AG.
Valcárcel et al., Heidelberg, Germany. In Nature, 2000
The protein Sex-lethal (SXL) controls dosage compensation in Drosophila by inhibiting the splicing and translation of male-specific-lethal-2 (msl-2) transcripts.
The regulation of the Drosophila msl-2 gene reveals a function for Sex-lethal in translational control.
Baker et al., Stanford, United States. In Cell, 1997
Dosage compensation is restricted to males by the splicing regulator Sex-lethal, which functions to prevent the production of the MSL-2 protein in females by an unknown mechanism.
Dosage compensation and chromatin structure in Drosophila.
Baker et al., Stanford, United States. In Curr Opin Genet Dev, 1996
The molecular characterization of the msl-2 gene has, to a great extent, solved the question of how msl-mediated dosage compensation is restricted to males.
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